Voet Biochemistry 3e © 2004 John Wiley & Sons, Inc. Figure 19-1aClassification of hormones. (a)...
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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
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Transcript of Voet Biochemistry 3e © 2004 John Wiley & Sons, Inc. Figure 19-1aClassification of hormones. (a)...
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Figure 19-1a Classification of hormones. (a) Endocrine signals are directed at distant cells through the intermediacy of the bloodstream.
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Figure 19-1b Classification of hormones. (b) Paracrine signals are directed at nearby cells.
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Figure 19-1c Classification of hormones. (c) Autocrine signals are directed at the cell that produced them.
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Figure 19-2 Major glands of the human endocrine system.
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Figure 19-3a Binding of ligand to receptor. (a) A hyperbolic plot.
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Figure 19-3b Binding of ligand to receptor. (b) A Scatchard plot.
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Figure 19-4 Biosynthesis of T3 and T4 in the thyroid gland.
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Figure 19-5 The roles of PTH, vitamin D, and calcitonin in controlling Ca2+ metabolism.
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Figure 19-6 Activation of vitamin D3 as a hormone in liver and kidney.
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Figure 19-7 Hormonal control circuits, indicating the relationships between the hypothalamus, the pituitary, and the target tissues.
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Figure 19-8 Patterns of hormone secretion during the menstrual cycle in the human female.
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Figure 19-9 X-Ray structure of human growth hormone (hGH) in complex with two molecules of its receptor’s extracellular domain (hGHbp).
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Figure 19-10 Acromegaly.
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Figure 19-11 The NO synthase (NOS) reaction.
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Figure 19-12 X-Ray structure of the oxygenase domain of iNOS.
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Figure 19-13 Activation/deactivation cycle for hormonally stimulated AC.
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Figure 19-14 General structure of a G protein-coupled receptor (GPCR).
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Figure 19-15 X-Ray structure of bovine rhodopsin.
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Figure 19-16 Mechanism of receptor-mediated activation/ inhibition of AC.
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Figure 19-17a Structural differences between the inactive and active forms of Gt (transducin). (a) Gt·GDP ribbon form.
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Figure 19-17b Structural differences between the inactive and active forms of Gt (transducin). (b) Gt·GDP spacing-filling form.
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Figure 19-17c Structural differences between the inactive and active forms of Gt (transducin). (c) Gt·GTPS ribbon form.
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Figure 19-17d Structural differences between the inactive and active forms of Gt (transducin). (d) Gt·GTPS spacing-filling form.
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Figure 19-18a X-Ray structure of the heterotrimeric G protein Gi.
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Figure 19-18b X-Ray structure of the heterotrimeric G protein Gi. (b) View related to that in Part a by a 90° rotation.
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Figure 19-19 Mechanism of action of cholera toxin.
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Figure 19-20a X-Ray structure of cholera toxin.
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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.
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Figure 19-21 Schematic diagram of a typical mammalian AC.
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Figure 19-22 The X-ray structure of an AC catalytic core.
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Figure 19-23 Domain organization in a variety of receptor tyrosine kinase (RTK) subfamilies.
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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.
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Figure 19-25 Schematic diagrams of RTKs.
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Figure 19-26a X-Ray structure of the PTK domain of the insulin receptor.
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Figure 19-26b X-Ray structure of the PTK domain of the insulin receptor.
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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.
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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.
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Figure 19-28 Variation of the cancer death rate in humanswith age.
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Figure 19-29a Transformation of cultured chicken fibroblasts by Rous sarcoma virus. (a) Normal cells adhere to the surface of the culture dish.
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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.
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Figure 19-30 The two-hybrid system.
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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.
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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.
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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.
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Figure 19-33 X-Ray structure of the SH3 domain from Abl protein in complex with its 10-residue target Pro-rich polypeptide (APTMPPPLPP).
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Figure 19-34 X-Ray structure of Grb2.
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Figure 19-35 Structure of an insulin receptor substrate protein.
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Figure 19-36 X-Ray structure of the complex between Ras and the GEF-containing region of Sos.
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Figure 19-38 The Ras-activated MAP kinase cascade.
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Figure 19-39 X-Ray structure of the Ras binding domain of Raf (RafRBD; orange) in complex with Rap1A·GDPNP (light blue).
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Figure 19-40 MAP kinase cascades in mammalian cells.
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Figure 19-41a Some examples of scaffold proteins that modulate mammalian MAP kinase cascades. (a) JIP-1.
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Figure 19-41b Some examples of scaffold proteins that modulate mammalian MAP kinase cascades. (b) MEKK1.
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Figure 19-42 Domain organization of the major NRTK subfamilies.
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Figure 19-43 X-Ray structure of Src·ADPNP lacking its N-terminal domain and with Tyr 527 phosphorylated.
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Figure 19-44a Schematic model of Src activation.
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Figure 19-44b Schematic model of Src activation.
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Figure 19-45 The JAK-STAT pathway for the intracellular relaying of cytokine signals.
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Figure 19-46 X-Ray structure of the Abl PTK domain in complex with a truncated derivative of gleevec.
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Figure 19-47 X-Ray structure of the protein tyrosine phosphatase SHP-2.
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Figure 19-48 X-Ray structure of the A subunit of PP2A.
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Figure 19-49a Calcineurin. (a) X-Ray structure of human FKBP12·FK506–CaN.
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Figure 19-49b Calcineurin. (b) X-Ray structure of human CaN with CaNA yellow, its autoinhibitory segment red, and CaNB cyan.
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Figure 19-50 Molecular formula of the phosphatidylinositides.
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Figure 19-51 Role of PIP2 in intracellular signaling.
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Figure 19-52 A phospholipase is named according to the bond that it cleaves on a glycerophospholipid.
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Figure 19-53 Domain organization of the four classes of phosphoinositide-specific PLCs.
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Figure 19-54 X-Ray structure of phospholipase C-1 lacking its N-terminal PH domain in complex with PIP3 and Ca2+ ions.
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Figure 19-55 X-Ray structure of the pleckstrin homology domain of PLC-1 in complex with PIP3.
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Figure 19-56 X-Ray structure of the C1B motif of PKC in complex with phorbol-13-acetate.
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Figure 19-57 Activation of PKC.
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Figure 19-58 Flow chart of reactions in the synthesis of phosphoinositides in mammalian cells.
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Figure 19-59 Domain organization of the 3 classes of PI3Ks.
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Figure 19-60 X-Ray structure of PI3K·ATP.
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Figure 19-61 X-Ray structure of PI3K–Ras·GDPNP.
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Figure 19-62 NMR structure of the EEA1 FYVE domain in complex with PtdIns-3-P.
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Figure 19-63 X-Ray structure of PTEN.
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Figure 19-64 Insulin signal transduction.
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Table 19-1 Some Human Hormones – Polypeptides.
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Table 19-1 (continued) Some Human Hormones – Polypeptides.
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Table 19-1 (continued) Some Human Hormones – Steroids.
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Table 19-1 (continued) Some Human Hormones – Amino Acid Derivatives.
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