Page 658 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-1a Classification of hormones. (a) Endocrine signals are directed at distant cells through the intermediacy of the bloodstream.

Page 658 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-1b Classification of hormones. (b) Paracrine signals are directed at nearby cells.

Page 658 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-1c Classification of hormones. (c) Autocrine signals are directed at the cell that produced them.

Figure 19-2 Major glands of the human endocrine system. Page 658 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-2 Major glands of the human endocrine system.

Figure 19-3a Binding of ligand to receptor. (a) A hyperbolic plot. Page 660 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-3a Binding of ligand to receptor. (a) A hyperbolic plot.

Figure 19-3b Binding of ligand to receptor. (b) A Scatchard plot. Page 660 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-3b Binding of ligand to receptor. (b) A Scatchard plot.

Figure 19-4 Biosynthesis of T3 and T4 in the thyroid gland. Page 662 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-4 Biosynthesis of T3 and T4 in the thyroid gland.

Page 663 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-5 The roles of PTH, vitamin D, and calcitonin in controlling Ca2+ metabolism.

Figure 19-6 Activation of vitamin D3 as a hormone in liver and kidney. Page 665 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-6 Activation of vitamin D3 as a hormone in liver and kidney.

Page 668 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-7 Hormonal control circuits, indicating the relationships between the hypothalamus, the pituitary, and the target tissues.

Page 669 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-8 Patterns of hormone secretion during the menstrual cycle in the human female.

Page 670 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-9 X-Ray structure of human growth hormone (hGH) in complex with two molecules of its receptor’s extracellular domain (hGHbp).

Figure 19-10 Acromegaly. Page 670 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-10 Acromegaly.

Figure 19-11 The NO synthase (NOS) reaction. Page 671 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-11 The NO synthase (NOS) reaction.

Figure 19-12 X-Ray structure of the oxygenase domain of iNOS. Page 672 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-12 X-Ray structure of the oxygenase domain of iNOS.

Page 674 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-13 Activation/deactivation cycle for hormonally stimulated AC.

Figure 19-14 General structure of a G protein-coupled receptor (GPCR). Page 674 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-14 General structure of a G protein-coupled receptor (GPCR).

Figure 19-15 X-Ray structure of bovine rhodopsin. Page 675 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-15 X-Ray structure of bovine rhodopsin.

Page 676 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-16 Mechanism of receptor-mediated activation/ inhibition of AC.

Page 678 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-17a Structural differences between the inactive and active forms of Gta (transducin). (a) Gta·GDP ribbon form.

Page 678 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-17b Structural differences between the inactive and active forms of Gta (transducin). (b) Gta·GDP spacing-filling form.

Page 678 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-17c Structural differences between the inactive and active forms of Gta (transducin). (c) Gta·GTPgS ribbon form.

Page 678 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-17d Structural differences between the inactive and active forms of Gta (transducin). (d) Gta·GTPgS spacing-filling form.

Figure 19-18a X-Ray structure of the heterotrimeric G protein Gi. Page 679 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-18a X-Ray structure of the heterotrimeric G protein Gi.

Page 679 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-18b X-Ray structure of the heterotrimeric G protein Gi. (b) View related to that in Part a by a 90° rotation.

Figure 19-19 Mechanism of action of cholera toxin. Page 680 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-19 Mechanism of action of cholera toxin.

Figure 19-20a X-Ray structure of cholera toxin. Page 681 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-20a X-Ray structure of cholera toxin.

Page 681 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e 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.

Figure 19-21 Schematic diagram of a typical mammalian AC. Page 682 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-21 Schematic diagram of a typical mammalian AC.

Figure 19-22 The X-ray structure of an AC catalytic core. Page 682 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-22 The X-ray structure of an AC catalytic core.

Page 684 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-23 Domain organization in a variety of receptor tyrosine kinase (RTK) subfamilies.

Page 685 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e 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.

Figure 19-25 Schematic diagrams of RTKs. Page 686 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-25 Schematic diagrams of RTKs.

Page 687 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-26a X-Ray structure of the PTK domain of the insulin receptor.

Page 687 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-26b X-Ray structure of the PTK domain of the insulin receptor.

Page 688 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e 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 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e 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.

Figure 19-28 Variation of the cancer death rate in humans with age. Page 688 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-28 Variation of the cancer death rate in humans with age.

Page 689 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e 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 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e 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.

Figure 19-30 The two-hybrid system. Page 690 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-30 The two-hybrid system.

Page 691 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e 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 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e 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 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e 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 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-33 X-Ray structure of the SH3 domain from Abl protein in complex with its 10-residue target Pro-rich polypeptide (APTMPPPLPP).

Figure 19-34 X-Ray structure of Grb2. Page 694 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-34 X-Ray structure of Grb2.

Figure 19-35 Structure of an insulin receptor substrate protein. Page 694 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-35 Structure of an insulin receptor substrate protein.

Page 695 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-36 X-Ray structure of the complex between Ras and the GEF-containing region of Sos.

Figure 19-38 The Ras-activated MAP kinase cascade. Page 696 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-38 The Ras-activated MAP kinase cascade.

Page 697 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-39 X-Ray structure of the Ras binding domain of Raf (RafRBD; orange) in complex with Rap1A·GDPNP (light blue).

Figure 19-40 MAP kinase cascades in mammalian cells. Page 698 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-40 MAP kinase cascades in mammalian cells.

Page 699 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-41a Some examples of scaffold proteins that modulate mammalian MAP kinase cascades. (a) JIP-1.

Page 699 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-41b Some examples of scaffold proteins that modulate mammalian MAP kinase cascades. (b) MEKK1.

Figure 19-42 Domain organization of the major NRTK subfamilies. Page 700 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-42 Domain organization of the major NRTK subfamilies.

Page 700 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-43 X-Ray structure of Src·ADPNP lacking its N-terminal domain and with Tyr 527 phosphorylated.

Figure 19-44a Schematic model of Src activation. Page 701 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-44a Schematic model of Src activation.

Figure 19-44b Schematic model of Src activation. Page 701 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-44b Schematic model of Src activation.

Page 702 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-45 The JAK-STAT pathway for the intracellular relaying of cytokine signals.

Page 703 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-46 X-Ray structure of the Abl PTK domain in complex with a truncated derivative of gleevec.

Page 705 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-47 X-Ray structure of the protein tyrosine phosphatase SHP-2.

Figure 19-48 X-Ray structure of the A subunit of PP2A. Page 706 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-48 X-Ray structure of the A subunit of PP2A.

Page 707 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-49a Calcineurin. (a) X-Ray structure of human FKBP12·FK506–CaN.

Page 707 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-49b Calcineurin. (b) X-Ray structure of human CaN with CaNA yellow, its autoinhibitory segment red, and CaNB cyan.

Figure 19-50 Molecular formula of the phosphatidylinositides. Page 707 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-50 Molecular formula of the phosphatidylinositides.

Figure 19-51 Role of PIP2 in intracellular signaling. Page 708 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-51 Role of PIP2 in intracellular signaling.

Page 709 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-52 A phospholipase is named according to the bond that it cleaves on a glycerophospholipid.

Page 709 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-53 Domain organization of the four classes of phosphoinositide-specific PLCs.

Page 710 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e 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 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-55 X-Ray structure of the pleckstrin homology domain of PLC-d1 in complex with PIP3.

Page 712 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-56 X-Ray structure of the C1B motif of PKC in complex with phorbol-13-acetate.

Figure 19-57 Activation of PKC. Page 713 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-57 Activation of PKC.

Page 714 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-58 Flow chart of reactions in the synthesis of phosphoinositides in mammalian cells.

Figure 19-59 Domain organization of the 3 classes of PI3Ks. Page 714 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-59 Domain organization of the 3 classes of PI3Ks.

Figure 19-60 X-Ray structure of PI3Kg·ATP. Page 715 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-60 X-Ray structure of PI3Kg·ATP.

Figure 19-61 X-Ray structure of PI3Kg–Ras·GDPNP. Page 715 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-61 X-Ray structure of PI3Kg–Ras·GDPNP.

Page 716 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-62 NMR structure of the EEA1 FYVE domain in complex with PtdIns-3-P.

Figure 19-63 X-Ray structure of PTEN. Page 718 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-63 X-Ray structure of PTEN.

Figure 19-64 Insulin signal transduction. Page 719 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Figure 19-64 Insulin signal transduction.

Table 19-1 Some Human Hormones – Polypeptides. Page 659 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Table 19-1 Some Human Hormones – Polypeptides.

Table 19-1 (continued) Some Human Hormones – Polypeptides. Page 659 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Table 19-1 (continued) Some Human Hormones – Polypeptides.

Table 19-1 (continued) Some Human Hormones – Steroids. Page 659 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Table 19-1 (continued) Some Human Hormones – Steroids.

Table 19-1 (continued) Some Human Hormones – Amino Acid Derivatives. Page 659 © 2004 John Wiley & Sons, Inc. Voet Biochemistry 3e Table 19-1 (continued) Some Human Hormones – Amino Acid Derivatives.