22c

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Page 658
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-1a Classification of hormones. (a) Endocrine
signals are directed at distant cells through the intermediacy
of the bloodstream.
Page 658
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-1b Classification of hormones. (b) Paracrine
signals are directed at nearby cells.
Page 658
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-1c Classification of hormones. (c) Autocrine
signals are directed at the cell that produced them.
Page 658
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-2
Major glands of the human endocrine system.
Page 660
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-3a Binding of ligand to receptor. (a) A hyperbolic
plot.
Page 660
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-3b Binding of ligand to receptor. (b) A Scatchard
plot.
Page 662
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-4
Biosynthesis of T3 and T4 in the thyroid gland.
Page 663
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-5 The roles of PTH, vitamin D, and calcitonin in
controlling Ca2+ metabolism.
Page 665
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-6
and kidney.
Activation of vitamin D3 as a hormone in liver
Page 668
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-7 Hormonal control circuits, indicating the
relationships between the hypothalamus, the pituitary, and
the target tissues.
Page 669
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-8 Patterns of hormone secretion during the
menstrual cycle in the human female.
Page 670
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-9 X-Ray structure of human growth hormone
(hGH) in complex with two molecules of its receptor’s
extracellular domain (hGHbp).
Page 670
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-10 Acromegaly.
Page 671
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-11 The NO synthase (NOS) reaction.
Page 672
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-12 X-Ray structure of the oxygenase domain of
iNOS.
Page 674
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-13 Activation/deactivation cycle for hormonally
stimulated AC.
Page 674
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-14 General structure of a G protein-coupled
receptor (GPCR).
Page 675
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-15 X-Ray structure of bovine rhodopsin.
Page 676
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-16 Mechanism of receptor-mediated activation/
inhibition of AC.
Page 678
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-17a Structural differences between the inactive
and active forms of Gta (transducin). (a) Gta·GDP ribbon
form.
Page 678
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-17b Structural differences between the inactive
and active forms of Gta (transducin). (b) Gta·GDP spacingfilling form.
Page 678
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-17c Structural differences between the inactive
and active forms of Gta (transducin). (c) Gta·GTPgS ribbon
form.
Page 678
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-17d Structural differences between the inactive
and active forms of Gta (transducin). (d) Gta·GTPgS spacingfilling form.
Page 679
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-18a X-Ray structure of the heterotrimeric G
protein Gi.
Page 679
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-18b X-Ray structure of the heterotrimeric G
protein Gi. (b) View related to that in Part a by a 90° rotation.
Page 680
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-19 Mechanism of action of cholera toxin.
Page 681
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-20a X-Ray structure of cholera toxin.
Page 681
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-20b X-Ray structure of cholera toxin. (b) The
structure of only the B5 pentamer in which each subunit is
binding CT’s GM1 receptor pentasaccharide.
Page 682
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-21 Schematic diagram of a typical mammalian
AC.
Page 682
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-22 The X-ray structure of an AC catalytic core.
Page 684
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-23 Domain organization in a variety of receptor
tyrosine kinase (RTK) subfamilies.
Page 685
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-24 The X-ray structure of the 2:2:2 complex of
FGF2, the D2–D3 portion of FGFR1, and a heparin
decasaccharide.
Page 686
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-25 Schematic diagrams of RTKs.
Page 687
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-26a X-Ray structure of the PTK domain of the
insulin receptor.
Page 687
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-26b X-Ray structure of the PTK domain of the
insulin receptor.
Page 688
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-27a Growth pattern of vertebrate cells in culture.
(a) Normal cells stop growing through contact inhibition once
they have formed a confluent monolayer.
Page 688
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-27b Growth pattern of vertebrate cells in culture.
(b) In contrast, transformed cells lack contact inhibition; they
pile up to form a multilayer.
Page 688
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-28 Variation of the cancer death rate in humans
with age.
Page 689
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-29a Transformation of cultured chicken
fibroblasts by Rous sarcoma virus. (a) Normal cells adhere to
the surface of the culture dish.
Page 689
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-29b Transformation of cultured chicken
fibroblasts by Rous sarcoma virus. (b) On infection with RVS,
these cells become rounded and cluster together in piles.
Page 690
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-30 The two-hybrid system.
Page 691
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-31a X-Ray structure of the 104-residue Src SH2
domain in complex with an 11-residue polypeptide containing
the protein’s pYEEI target tetrapeptide.
Page 691
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-31b X-Ray structure of the 104-residue Src SH2
domain in complex with an 11-residue polypeptide containing
the protein’s pYEEI target tetrapeptide.
Page 692
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-32 The NMR structure of the PTB domain of Shc
in complex with a 12-residue polypeptide from the Shc
binding site of a nerve growth factor (NGF) receptor.
Page 693
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-33 X-Ray structure of the SH3 domain from Abl
protein in complex with its 10-residue target Pro-rich
polypeptide (APTMPPPLPP).
Page 694
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-34 X-Ray structure of Grb2.
Page 694
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-35 Structure of an insulin receptor substrate
protein.
Page 695
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-36 X-Ray structure of the complex between Ras
and the GEF-containing region of Sos.
Page 696
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-38 The Ras-activated MAP kinase cascade.
Page 697
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-39 X-Ray structure of the Ras binding domain of
Raf (RafRBD; orange) in complex with Rap1A·GDPNP (light
blue).
Page 698
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-40 MAP kinase cascades in mammalian cells.
Page 699
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-41a Some examples of scaffold proteins that
modulate mammalian MAP kinase cascades. (a) JIP-1.
Page 699
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-41b Some examples of scaffold proteins that
modulate mammalian MAP kinase cascades. (b) MEKK1.
Page 700
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-42 Domain organization of the major NRTK
subfamilies.
Page 700
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-43 X-Ray structure of Src·ADPNP lacking its Nterminal domain and with Tyr 527 phosphorylated.
Page 701
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-44a Schematic model of Src activation.
Page 701
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-44b Schematic model of Src activation.
Page 702
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-45 The JAK-STAT pathway for the intracellular
relaying of cytokine signals.
Page 703
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-46 X-Ray structure of the Abl PTK domain in
complex with a truncated derivative of gleevec.
Page 705
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-47 X-Ray structure of the protein tyrosine
phosphatase SHP-2.
Page 706
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-48 X-Ray structure of the A subunit of PP2A.
Page 707
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-49a Calcineurin. (a) X-Ray structure of human
FKBP12·FK506–CaN.
Page 707
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-49b Calcineurin. (b) X-Ray structure of human
CaN with CaNA yellow, its autoinhibitory segment red, and
CaNB cyan.
Page 707
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-50 Molecular formula of the phosphatidylinositides.
Page 708
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-51 Role of PIP2 in intracellular signaling.
Page 709
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-52 A phospholipase is named according to the
bond that it cleaves on a glycerophospholipid.
Page 709
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-53 Domain organization of the four classes of
phosphoinositide-specific PLCs.
Page 710
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-54 X-Ray structure of phospholipase C-d1 lacking
its N-terminal PH domain in complex with PIP3 and Ca2+ ions.
Page 711
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-55 X-Ray structure of the pleckstrin homology
domain of PLC-d1 in complex with PIP3.
Page 712
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-56 X-Ray structure of the C1B motif of PKC in
complex with phorbol-13-acetate.
Page 713
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-57 Activation of PKC.
Page 714
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-58 Flow chart of reactions in the synthesis of
phosphoinositides in mammalian cells.
Page 714
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-59 Domain organization of the 3 classes of
PI3Ks.
Page 715
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-60 X-Ray structure of PI3Kg·ATP.
Page 715
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-61 X-Ray structure of PI3Kg–Ras·GDPNP.
Page 716
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-62 NMR structure of the EEA1 FYVE domain in
complex with PtdIns-3-P.
Page 718
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-63 X-Ray structure of PTEN.
Page 719
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Figure 19-64 Insulin signal transduction.
Page 659
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Table 19-1
Some Human Hormones – Polypeptides.
Page 659
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Table 19-1 (continued) Some Human Hormones –
Polypeptides.
Page 659
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Table 19-1 (continued) Some Human Hormones – Steroids.
Page 659
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.
Table 19-1 (continued) Some Human Hormones – Amino
Acid Derivatives.
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