Trace residues ranked in the top 20% of importance in classA GPCRs with predominantly G-protein
coupling mutational effect (updated February 2010, Rong Yao)
Column 1: B-W#
Column 2: Bovine rhodopsin residue numbering, ET evolutionary coverage (prET coverage)
Column 3: Actual mutation in the cited work (residue number is that of the receptor family in which the experiment was done).
Column 4: Receptor family.
Column 5: Reference.
Column 6: Functional assay(s).
Column 7: Effect.
Column 8: Magnitude of mutational effect.
Column 9: Interpretation.
Color codes:
Green: G-protein coupling effects:
Red: Internalization/sequestration effects
Yellow: No functional effect.
Grey: Mutation cited is not a point mutation. Either a multiple substitution or mutated in presence of another agent such as Zn ions.
B-W#
Rhod#
B2-adr#
ClassA ET
Rank (prET
Rank, use
1f88as ref)
Mutated
to
2.39
L72
T68
16% (5%)
L72A
Rhodopsin
(1)
Light dependent GTPS binding to Gt
T109A
Serotonin type 2
5HT2A_RAT
(41)
Agonist-induced receptor desensitization was assessed
PI hydrolysis assay
M73K
3.51
3.53
Y136
Y132
22%(16%)
V138
A134
15% (9%)
Receptor family
Refere
nce
Y127A
Mouse receptor MC1-R
MSHR_SHEEP
Angiotensin-2 receptor
(42)
Y135A
Y139F
CXCR4 receptor
CCR2 receptor
(3)
(4)
Y127H
AT1 receptor
(5)
Y136A
IL-8 receptor
(6)
S140F
GNRH receptor
(7)
(2)
Functional Assay
Into mouse receptor(mMC1-R) for pharmacological
analysis
(1) [cAMP] on forskolin stim.
(2) Effect of [GTPS] on angiotensin-2 binding.
(3) [Ca2+] or [IP]
Fluorescent antibody staining. (DRY motif mutated)
Ca2+ mobilization using flow cytometry.
Phosphorylation & association with Janus Kinase-2
using Western Blot. Phosphorylation. Site.
Following AT-2 stimulation IP prodn. in
presence/absence of ZnCl2 to build metal bridge.
Ca2+ mobilization in response to IL-8 (in combo with
other neighboring mutants)
Measured % of bound radioligand internalized.
Y132A
CXCR-4 receptor
(8)
Flow cytometry (DRY  NAA motif mutant)
Y127A
CCR5 receptor
(55)
Inositol phosophate assay (DRY->GGA motif mutant)
Effect
Magnitude of
effect
 Gt Activity. Kinase
phosphorylation.unaffected
Efficacy of 5-HT stimulated
PI hydrolysis-> no affect
potency of 5HT stimulating
PI hydrolysis
Constitutive activation
27%  (++)
G-protein coupling
No effect
desensitization
(+)
CA
Small  [cAMP]
No effect
 in [IP]
 Expression
 [Ca2+]
No phosphorylation
(+)
(-)
90%  (+++)
98%  (+++)
60%  (+++)
(+++)
G-protein coupling
 [IP]
70%  (+++)
 [Ca2+]
(+++)
No metal
bridge/Gq coupling
Giα coupling
 Internalization, recycling,
degradation,
 expression
[IP] production
(+)
Internalization
No effect
Prevent coupling to G-alpha
agonist-dependent
intracellular calcium
mobilization and chemotaxis
(-)
Not reqd. for coreceptor function

G-protein coupling
G-protein coupling
G-protein
specificity
10 fold 
β2 adrenergic receptor
(9)
Binding of [35S]GTPS to αs in presence of Zn.
 G-protein coupling
V138H
Rhodopsin
(10)
Binding of [35S]GTPS to αs in presence of Zn.
 transducin activation.
10 fold 
(+++)
50%  (+++)
S134A
α2A adrenergic receptor
(11)
Change in response
(+)
A129H
AngiotensinII type1 receptor
Melanocortin receptor
(43)
Biphasic response to NE. Forskolin stimulated [cAMP]
(in association with L143S)
Ligand binding and stimulate IP production in COS cell
Stable and transient luciferase expression activity
 in [IP]
(+)
 receptor activation
 intermediate reduction in
receptor binding
Complete failure of
mediating ligand-provoked
Gs activation
(+)
T470A
(44)
Follicle stimulating
hormone receptor
FSH-stimulated cAMP level
(45)
Expression
Kinase coupling
(+)
A134H
T150I
Comments
(++++)
G-protein coupling
G-protein coupling
5.58
6.37
7.53
Y223
Y219
6% (25%)
V254
L275
13%
(15%)
Y306
Y226
2% (1%)
Y216A
Neurokinin-1 receptor
(12)
Substance-P (SP) stimulated accumulation of IP.
Loss of PI hydrolysis.
Ligand binding specificity
(++++)
(++)
Y601A/
D/F/H/K
/PSW
Y215F
Thyrotropin receptor
(13)
(1) cAMP production.
(2) TSH induced PI hydrolysis.
Effects vary for different
mutations.
 cAMP
(+++)
Angiotensin-2 receptor
(14)
M2-Muscarinic
(15)
 Affinity for AT-2.
 in internalization
 G-protein coupling
(+++)
V385A
T410P
PTH receptor
(16)
Opossum receptor homolog
Secretin receptor
(17)
(18)
[cAMP] levels
[IP] levels
 [cAMP]
 [cAMP]
4X  (++)
(+++)
T410P
T322P
I125-AT-2 used to measure internalization rates and AT2 binding. IP response studies for signaling.
Ability to inhibit cAMP production using [cAMP]
assay.(VTIL AALS motif)
[cAMP] & [IP] accumulation assays. Mutation causes
Jansen's Metaphyseal Chondrodysplasia
[cAMP] accumulation
[cAMP] accumulation
T352S
T352P
T352A
Glucagon receptor
(19)
(1) Competition binding of 125I-glucagon
(2) Glucagon induced [cAMP] accumulation
(3) [cAMP] accumulation
 [125I-glucagon] binding
 Glucagon potency
 AC activity
40%  (+++)
5X  (++)
3.7X  (++)
Ligand binding
T343/K/
P/A
L492S
VIP receptor
(20)
[cAMP] accumulation
M3/M2 muscarinic
acetylcholine receptor
(21)
Carbachol stimulated [IP] levels.
 [cAMP]
 [IP1] w.r.t M2
3.5X  (++)
2X  (++)
V385A
M2 muscarinic receptor
(22)
PI hydrolysis (point mutation and VTILAALS motif
 [IP]
6 X  (+++)
G protein coupling
Receptor signaling
changed from
M3M2. Gq/G11
activation.
G-protein coupling
/specificity
V385A
M2 muscarinic receptor
(23)
PI hydrolysis and cAMP assays. Insertion mutagenesis
N and C terminal to VTIL motif.
[IP]
[cAMP]
(++)
40%  (+++)
4.5X  (++)
Receptors
conformation
adjustable for new
ligands
Gs coupling
Internalization &
G protein coupling
G protein coupling
G protein coupling
G protein coupling
G protein coupling
G protein coupling
G-protein coupling
and activation
Knocked out
agonist induced
redistribution.
Y348A
α1B adrenergic receptor
(24)
PI hydrolysis, intracellular Ca2+ mobilization.
Sucrose density gradient for receptor
expression/distribution.
Loss of PI hydrolysis
Ca2+ mobilization.
Expression
100% (++++)
100% (++++)
 (+)
Y326A
β2 adrenergic receptor
(25)
Lutropin receptor
(26)
Abolished Sequestration
No change.
cAMP response lost
Ligand Binding
(++++)
(-)
(+++)
(-)
Sequestration
Y601A
(1) Seq. I125 pindolol radioligand binding. (2)
Isoproterenol stimulated AC activity.
HcG induced cAMP assay
Y302F/
A
Angiotensin 2
(27)
AT-2 induced IP3 production.
[IP3] abolished
no change internalization
(+++)
(-)
G-protein coupling
Y306C
Rhodopsin
(28)
Gt activation using fluorescence spectroscopy
No G activation
(+++)
G-protein coupling
Y293FY
293A
PAF
(29)
(1) 3H-PAF  liquid scintillation for internalization
rates
(2) IP accumulation for signaling effects
No change in [IP]
Abolished G-protein
signaling
No internalization effect
(-)
(+++)
No effect.
G-protein coupling
(-)
Receptor
signaling ME
7.57
N310
P330
9% (8%)
Y326A
Y293A
Y302F
β2 adrenergic receptor
PAF receptor
Lipoxin A4 receptor
(30)
(31)
(32)
SequestrationI125 pindolol radioligand binding
Competition binding with 3H-PAF and IP production.
PhospholipaseD, A2 activation assay & Western
blotting
Y371A
Thrombin receptor
(33)
Ca2+ release. Triple mutant along with Y372A, Y373A
Y322F
Y322A
Gonadotropin releasing
Hormone
(34)
IP production assay. Effects of GTPyS on [125I]GnRHAg Binding to GnRH Receptors
Y297A
CCR5 receptor
(36)
Y386A
CCK type A receptor
(37)
Y324A
Gastrin releasing peptide
receptor
(38)
Y302A
Angiotensin 2
(39)
Entry of HIV- viruses into cells using a luciferasebased reporter assay
Internalization fluorescent probes
Ligand binding radioligand binding.
Ligand binding Gastric Release Peptide (GRP)
binding
Ca2+ dose response to GRP.
125I-GRP internalization
125I-AT-2 radioactivity in internalized vesicles.
Y288C
Adenosine receptor
(46)
Potency of receptor agonist C1-IB-MECA binding
Phospholipase C(PLC) and adenylyl cyclase (AC)
Y543H
Muscarinic acetylcholine
receptor M3
(47)
Evidenced by Carbachol potency level
Y332A
Bradykinin B2 receptor
(48)
Confocal fluorescence microscopy show Y305A-eGFP
chimera
Two dimentional phosphopeptide analysis show
constitutively exhibite a phosphorylation pattern
Accumulation rate of [IP] unchanged -> Precouple to
Gq/11 without activating G protein
cAMP accumulation
Y299A
Cannabinoid receptor
(49)
Y304A
Somatostatin receptor
(50)
Y305A/
F
Tachykinin receptor 1
(51)
Y325F
Vasopressin type2 receptor
(54)
N310C
Rhodopsin
Rhodopsin
(28)
(40)
G301V
Chemokine CCR5
(52)
Mutant exhibite surface immunofluorescence with
antibody
Immunofluorescence and confocal microscopy to
determine the effects of the mutations on the
subcellular distribution
Internalization of 125I-SP and cy3-SP
Plus deletion of tyrosine kinase domain -> cause
conformation change->endocytic motifs constitutively
Exposed
desensitization and resensitization assay->agonist
stimulation
preincubation of mutant receptor with AVP
Gt activation fluorescence spectroscopy
Peptide competing with rhodopsin-G interaction
measured using fluorescence spectroscopy
Coexpression of receptor with apoaequirin, binding
Slight  in sequestration
 [IP]
change in signaling due to
lack of phosphorylation by
GRK
Abolished Ca2+ release.
(+)
10%  (+)
(+++)
Sequestration
ME
Receptor
signaling ME
(+++)
Receptor signaling.
No effect
G-protein coupling and IP
response abolished
 internalization
No change
(-)
(+++)
No effect
G-protein coupling
 40% (+++)
(-)
Internalization
No effect
No change in fluorescence
(-)
No effect
No change in ligand binding
(-)
No effect
No change in internalization
(-)
No effect on
receptor
internalization.
potency or inactive
Follow 2 mutants in DRY
motif
 efficiency of agoinstinduced receptor G protein
coupling
Ligand-independent
phosphorylation and
internalization
 [cAMP]
Effect of anandamide is
complete abolished
CA
 100 fold
G-protein coupling
(+++)
G-protein coupling
Internalization
(+++)
G-protein coupling
Ligand binding
Internalization
Ligand binding
 internalization
 30%
Internalization
CA
As effective as wildtype
Lose little[3H]AVP binding
site at cell surface
Change in fluorescence
Change in fluorescence
No change
(-)

(++)
(++)
No affect
No effect on
agonist stimulation
internalization
G-protein
coupling
G-protein coupling
Ligand binding
K391A
Enlothelin B receptor
(53)
affinity for MIP-1beata with EC50
Immuno complex kinase assay -> measure catalytic
activity
 ERK activity
(+++)
Followings further identified by ET or prET
3.54
V139
I135
19%
(19%)
V127A
Muscarinic acetylcholine
receptor
(58)
Surface [3H] NMS binding assayed in Hm1 transfected
cells, PI coupling efficiency of mutants with detectable
receptor yield
Complete suppressed
sequestration and coupling of
Hm1
 (+++)
V147A
Alpha Adrenoceptors type1
(59)
Receptor expression measured by [125I]HEAT
Basal/epinephrine IP accumulation
 constitutive activity->
switch to active receptor
state
Entire abolish the
constitutive and agonistinduced activity
 reduce agonist-induced IP
signal generation

V147E
I130A
Alpha Adrenoceptors type1
Angiotensin type 1
(59)
(60)
Receptor expression measured by [125I]HEAT
Basal/epinephrine IP accumulation
Inositol phosphate measurement
Sequestration
CA
 receptor
mediated
signaling
 Gq coupling
Receptor function
G-protein coupling
No effect on
internalization
I143A
2.40
N73
N69
11%
(6%)
6.33
7.54
(734)
7.55
(735)
7.56
(736)
V250
A271
31%
(18%)
I307
C327
20%
(11%)
M308
R328
39%
(19%)
M309
S329
Gonadotropin releasing
hormone
(61)
I139A
CXCR1_HUMAN
(62)
N73A
E68S
OPSD_BOVIN
BKRB2_RAT
(63)
(64)
R450H
D83A
D83N
TSHR_Human
VG74_HHV8
(65)
(66)
D83A/
V142D
R335L
[125]I labeled receptor binding GnRH->Kd estimated
for competition binding
Phosphatidylinositol hydrolysis assay
 receptor activation
Involved in coupling IL8RA,B to Gi2, but groups
mutants
Involved in calcium mobilization
 calcium mobilization
 Gt activation
 ligand binding
 PI turn over
 ligand binding cAMP
more active than KSHV
Affinity for Gro alpha,
 basal signaling activity
more active , basal signaling

Receptor signaling
efficiency
G-protein coupling
G-protein coupling
Small 27%
60%
69%
Slightly
G-protein coupling
LB
G-protein coupling
LB/ G-protein
coupling
190% / 110%
CA
510%
CA
G-protein coupling
GASR_RAT
(cholecystokinin CCK)
(67)
Significantly reduction [IP] and [Ca++] dependent
current
K566A
LSHR_HUMAN
(68)
Increase basal [CAMP] level
CA
Q263E
Q263R
V323S
TRFR_MOUSE
(69)
Exhibite normal expression, binding affinity, signaling
No effect
(70)
Significantly reduce [IP] accumulation
(71)
Cause constitutive, ligand-independent signaling
I625K
BKRB1_RAT
(bradykinin receptor)
SMP_HUMAN
(smoothened family)
LSHR_PIG
(72)
Severely reduced signaling, impairment of LH receptor
function
I625K
LSHR_HUMAN
V388K
EDNRB_RAT
(endothelin B receptor)
W535L
(74,75
)
(73)
No effect on binding, but
↓[IP]
↓[IP]
CA
reduce cAMP synthesis
Severely inhibit ERK activation
G-protein coupling
Severely
Loss function
mildly
Impair of signaling
Severely
ERK activiation
21%
(14%)
REFERENCES:
1.
Wen Shi, S. O., Charlene D. Dickerson, and Ellen R. Weiss. (1995) J. Biol. Chem. 270, 2124-2132
2.
Shibata T, S. C., Ohnishi J, Murakami K, Miyazaki H. (1996) Biochem Biophys Res Commun 218(1), 383-9
3.
Chabot, D., Zhang PF, Quinnan GV, Broder CC. (1999) J Virol 73(8), 6598-6609
4.
Mellado, M., Rodriguez-Frade JM, Aragay A, del Real G, Martin AM, Vila-Coro AJ,, and Serrano A, M. F. J., Martinez-A C. (1998) J Immunology 161(2), 805-13
5.
Miura S, Z. J., Karnik SS. (2000) FEBS Lett 470(3), 331-5
6.
Damaj, B. B., McColl, S. R., Neote, K., Songqing, N., Ogborn, K. T., Hebert, C. A., and Naccache, P. H. (1996) Faseb J 10(12), 1426-34
7.
Byrne B, M. A., Taylor PL, Sellar R, Rodger FE, Fraser HM, Eidne KA. (1999) J Endocrinol 163(3), 447-56
8.
Lu Z, B. J., Chen Y, Turner JD, Zhang T, Sharron M, Jenks MH, Wang Z, Kim J,, and Rucker J, H. J., Peiper SC, Doms RW. (1997) PNAS 94(12), 6426-31
9.
Sheikh SP, V. J., Baranski TJ, Lichtarge O, Iiri T, Meng EC, Nissenson RA, Bourne HR. (1999) J. Biol. Chem. 274(24), 17033-41
10.
Sheikh SP, Z. T., Lichtarge O, Sakmar TP, Bourne HR. (1996) Nature 383(6598), 347-50
11.
Nasman J, J. C., Akerman KE. (1997) J Biol Chem 272(15), 9703-8
12.
Huang RR, H. D., Strader CD, Fong TM. (1995) Biochemistry 34(50), 16467-72
13.
Biebermann H, S. T., Schulz A, Krause G, Gruters A, Schultz G, GudermannT. (1998) FASEB J 12(14), 1461-71
14.
Hunyady L, M. B., Tamás Balla, and Kevin J. Catt. (1995) J Biol.Chem 270, 9702-9705
15.
Liu, J., Conklin, B. R., Blin, N., Yun, J., and Wess, J. (1995) Proc Natl Acad Sci U S A 92(25), 11642-6
16.
Schipani E, L. C., Parfitt AM, Jensen GS, Kikuchi S, Kooh SW, Cole WG, Juppner H. (1996) N Engl J Med 335(10), 708-14
17.
Schipani E, J. G., Pincus J, Nissenson RA, Gardella TJ, Juppner H. (1997) Mol Endocrinol 11(7), 851-8
18.
Ganguli SC, P. C., Holtmann MH, Hadac EM, Kenakin TP, Miller LJ. (1998) J Pharmacol Exp Ther 286(2), 593-8
19.
Hjorth SA, O. C., Schwartz TW. (1998) Mol Endocrinol 12(1), 78-86
20.
Gaudin P, C. A., Rouyer-Fessard C, Maoret JJ, Laburthe M. (1999) Biochem Biophys Res Commun 254(1), 15-20
21.
Blin N, Y. J., Wess J. (1995) J Biol Chem 270(30), 17741-8
22.
Kostenis E, C. B., Wess J. (1997) Biochemistry 36(6), 1487-95
23.
Liu, J., Blin, N., Conklin, B. R., and Wess, J. (1996) J Biol Chem 271(11), 6172-8
24.
Wang J, Z. J., Anderson JL, Toews ML. (1997) Mol Pharmacol 52(2), 306-13
25.
Barak LS, T. M., Freedman NJ, Kwatra MM, Lefkowitz RJ, Caron MG. (1994) J Biol Chem 269(4), 2790-5
26.
Fernandez LM, P. D. (1996) Biochemistry 35(13), 3986-93
27.
Laporte SA, S. G., Richard DE, Escher E, Guillemette G, Leduc R. (1996) Mol Pharmacol 49(1), 89-95
28.
Cai K, K.-S. J., Farrens D, Zhang C, Altenbach C, Hubbell WL, Khorana HG. (1999) Biochemistry 38(25), 7925-30
29.
Le Gouill C, P. J., Rola-Pleszczynski M, Stankova J. (1997) J Biol Chem 272(34), 21289-95
30.
Menard L, F. S., Zhang J, Lin FT, Lefkowitz RJ, Caron MG, Barak LS. (1997) Mol Pharmacol 51(5), 800-8
31.
Le Gouill C, P. J., Caron CA, Gaudreau R, Volkov L, Rola-Pleszczynski M,, and J., S. (1999) J Biol Chem 274(18), 12548-54
32.
Kang Y, T. B., Varai G, Varga J, Fiore S. (2000) Biochemistry 39(44), 13551-7
33.
Chen J, I. M., Wang L, Ishii K, Coughlin SR. (1994) J Biol Chem 269(23), 16041-5
34.
Arora KK, C. Z., Catt KJ. (1996) Mol Endocrinol 10(8), 979-86
35.
Chen S, X. M., Lin F, Lee D, Riek P, Graham RM. (1999) J Biol Chem 274(23), 16320-30
36.
Dragic T, T. A., Thompson DA, Cormier EG, Kajumo FA, Maxwell E, Lin SW, Ying, and W, S. S., Sakmar TP, Moore JP. (2000) PNAS 97(10), 5639-44
37.
Go WY, H. E., Hadac EM, Rao RV, Miller LJ. (1998) Am J Physiol 275(G56-62)
38.
Slice LW, W. H., Sternini C, Grady EF, Bunnett NW, Walsh JH. (1994) J Biol Chem 269(34), 21755-61
39.
Thomas WG, B. K., Motel TJ, Thekkumkara TJ. (1995) J Biol Chem 270(38), 22153-9
40.
Phillips, W. J., and Cerione, R. A. (1992) J Biol Chem 267(24), 17032-9
41.
Gray JA, Compton-Toth BA, Roth BL (2003) Biochemistry 42(36):10853-62
42.
Vage DI, Klungland H, Lu D, Cone RD (1999) Mamm Genome 10(1):39-43
43.
Miura S, Zhang J, Karnik SS (2000) FEBS Lett 470(3):331-5
44.
Vaisse C, Clement K, Durand E, Hercberg S, Guy-Grand B, Froguel P (2000)J Clin Invest 106(2):253-62
45.
Timossi C, Maldonado D, Vizcaino A, Lindau-Shepard B, Conn PM, Ulloa-Aguirre A (2002) Mol Cell Endocrinol 189(1-2):157-68
46.
Chen A, Gao ZG, Barak D, Liang BT, Jacobson KA (2001) Biochem Biophys Res Commun 284(3):596-601
47.
48.
49.
50.
51.
52.
53.
54.
55.
56.
57.
58.
59.
60.
61.
62.
63.
64.
65.
66.
67.
68.
69.
70.
71.
72.
73.
74.
75.
Schmidt C, Li B, Bloodworth L, Erlenbach I, Zeng FY, Wess J (2003) J Biol Chem 278(32):30248-60
Kalatskaya I, Schussler S, Blaukat A, Muller-Esterl W, Jochum M, Proud D, Faussner A (2004) J Biol Chem 279(30):31268-76
Feng W, Song ZH FEBS Lett (2001) 501(2-3):166-70
Hukovic N, Panetta R, Kumar U, Rocheville M, Patel YC (1998) J Biol Chem 273(33):21416-22
Bohm SK, Khitin LM, Smeekens SP, Grady EF, Payan DG, Bunnett NW (1997) J Biol Chem 272(4):2363-72
V, Vassart G, Doms RW, Parmentier M (2000) Blood 96(5):1638-45
Vichi P, Whelchel A, Posada J (1999) J Biol Chem 274(15):10331-8
Bouley R, Sun TX, Chenard M, McLaughlin M, McKee M, Lin HY, Brown D, Ausiello DA (2003) Am J Physiol Cell Physiol 285(4):C750-62. Epub 2003 Jun 11
Gosling J, Monteclaro FS, Atchison RE, Arai H, Tsou CL, Goldsmith MA, Charo IF (1997) Proc Natl Acad Sci U S A 94(10):5061-6
Shi W, Osawa S, Dickerson CD, Weiss ER (1995) J Biol Chem 270(5):2112-9
Howard OM, Shirakawa AK, Turpin JA, Maynard A, Tobin GJ, Carrington M, Oppenheim JJ, Dean M (1999) J Biol Chem 274(23):16228-34
Moro O, Shockley MS, Lameh J, Sadee W (1994) J Biol Chem 269(9):6651-5
Greasley PJ, Fanelli F, Scheer A, Abuin L, Nenniger-Tosato M, DeBenedetti PG, Cotecchia S (2001) J Biol Chem 276(49):46485-94
Gaborik Z, Jagadeesh G, Zhang M, Spat A, Catt KJ, Hunyady L (2003) Endocrinology 144(6):2220-8
Ballesteros J, Kitanovic S, Guarnieri F, Davies P, Fromme BJ, Konvicka K, Chi L, Millar RP, Davidson JS, Weinstein H, Sealfon SC (1998)
J Biol Chem 273:10445–10453
Identification of G-protein binding sites of the human interleukin-8 receptors by functional mapping of the intracellular loops.
Damaj BB, McColl SR, Neote K, Songqing N, Ogborn KT, Hebert CA, Naccache PH. FASEB J 1996 Oct;10(12):1426-34.
Rhodopsin mutants discriminate sites important for the activation of rhodopsin kinase and Gt.Shi W, Osawa S, Dickerson CD, Weiss ER
J Biol Chem 1995 Feb 3;270(5):2112-9.
Coulombic and hydrophobic interactions in the first intracellular loop are vital for bradykinin B2 receptor ligand binding and consequent signal
transduction.. Yu J, Polgar P, Lubinsky D, Gupta M, Wang L, Mierke D, Taylor L. Biochemistry 2005 Apr 12;44(14):5295-306.
Novel inactivating missense mutations in the thyrotropin receptor gene in Japanese children with resistance to thyrotropin. Nagashima T, Murakami M,
Onigata K, Morimura T, Nagashima K, Mori M, Morikawa A. Thyroid 2001 Jun;11(6):551-9.
Ho HH, Ganeshalingam N, Rosenhouse-Dantsker A, Osman R, Gershengorn MC. J Biol Chem 2001 Jan 12;276(2):1376-82.
Basic amino acids at the C-terminus of the third intracellular loop are required for the activation of phospholipase C by cholecystokinin-B receptors.
Wang HL. J Neurochem 1997 Apr;68(4):1728-35.
Requirement of specific intrahelical interactions for stabilizing the inactive conformation of glycoprotein hormone receptors. Schulz A, Bruns K,
Henklein P, Krause G, Schubert M, Gudermann T, Wray V, Schultz G, Schoneberg T. J Biol Chem 2000 Dec 1;275(48):37860-9.
Juxtamembrane regions in the third intracellular loop of the thyrotropin-releasing hormone receptor type 1 are important for coupling to Gq. Buck F,
Wang W, Harder S, Brathwaite C, Bruhn TO, Gershengorn MC. Endocrinology 2000 Oct;141(10):3717-22.
The role of helix 8 and of the cytosolic C-termini in the internalization and signal transduction of B(1) and B(2) bradykinin receptors. Faussner A,
Bauer A, Kalatskaya I, Schussler S, Seidl C, Proud D, Jochum M. FEBS J 2005 Jan;272(1):129-40.
Downregulation of Hedgehog signaling is required for organogenesis of the small intestine in Xenopus. Zhang J, Rosenthal A, de Sauvage FJ,
Shivdasani RA. Dev Biol 2001 Jan 1;229(1):188-202.
A homozygous mutation in the luteinizing hormone receptor causes partial Leydig cell hypoplasia: correlation between receptor activity and phenotype.
Martens JW, Verhoef-Post M, Abelin N, Ezabella M, Toledo SP, Brunner HG, Themmen AP 1998 Mol Endocrinol 12:775–784
Transmembrane helix 7 of the endothelin B receptor regulates downstream signaling. Vichi P, Whelchel A, Posada J. J Biol Chem 1999 Apr
9;274(15):10331-8.
Effect of activating and inactivating mutations on the phosphorylation and trafficking of the human lutropin/choriogonadotropin receptor.
Min L, Ascoli M. Mol Endocrinol 2000 Nov;14(11):1797-810.
Male pseudohermaphroditism due to inactivating luteinizing hormone receptor mutations. Wu SM, Chan WY. Arch Med Res 1999
Nov-Dec;30(6):495-500.