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Document Figure 3 Schematic representation of the structure of a TIM monomer. Helices and strands are labeled as H and B, respectively. The view is along the axis of the β barrel, into the active site. Key catalytic residues Lys13, His95, and Glu167 are shown along with the helix that binds the substrate phosphate and the flexible loop that covers the substrate during catalysis. Black dots indicate residues in contact with the second monomer of the enzyme. (From Ref.24. Copyright 1991 by Harcourt Brace.) Page 372 10 Å instead of the 15 Å in the closed loop conformation of the enzyme. In any case, selective inhibitor design for TIM appears to require de novo design as there are no leads known that interact with the Ala- Tyr region of the enzyme. B. Glyceraldehyde-3-Phosphate Dehydrogenase (GAPDH) Glyceraldehyde-3-phosphate dehydrogenase is a homotetramer that carries out the oxidative phosphorylation of glyceraldehyde-3-phosphate into 1,3-bisphos- phoglycerate. During this reaction NADH is formed. Each subunit of the enzyme consists of two domains and has an NAD + binding site. The N-terminal domain anchors the adenosine portion of the cofactor while the nicotinamide portion is involved in the catalytic reaction at the C-terminal domain. T. brucei http://legacy.netlibrary.com/nlreader/nlReader.dll?bookid=12640&filename=Page_372.html (1 of 2) [4/5/2004 5:34:37 PM]
Document Figure 4 Stereoview of superimposed TIM monomers, one with an open flexible loop (full black) and another one with a closed flexible loop (open gray). The loop location is marked by an asterisk. Note the proximity of the active site, indicated by the catalytic residues Lys13, His95, and Glu167 (all sterofigures in this paper were drawn with MOLSCRIPT [93]). http://legacy.netlibrary.com/nlreader/nlReader.dll?bookid=12640&filename=Page_373.html (1 of 2) [4/5/2004 5:36:17 PM] Page 373
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Structure-based Drug Design 14 Stru
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Document 2 Structural Studies of HI
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Document dine (3TC), and 2',3'-dide
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Document Analysis of various HIV-1
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Document Table 3 HIV-1 RT Amino Aci
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Document ever, once an NNRTI is bou
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Document Chris Tantillo. The work i
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Document Page 72 16. Goldman ME, Nu
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Document reverse transcriptase inhi
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Document dine) and didanosine (dide
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Document -62° for HIV-1 integrase,
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Document proposed mechanisms. For e
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Document Page 106 on the same ring
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Document Page 108 mulate during tre
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Document when metals are bound. Fin
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Document cubation of phosphotyrosin
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Document 4 Bradykinin Receptor Anta
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Document Page 121 Nearly all cells
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Document Page 123 were poorly satis
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Document Page 125 binding site on t
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Document Page 127 The des-Arg 9 for
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Document receptor, it has not yet b
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Document Page 135 might be jointly
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Document Page 137 observed for the
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Document Figure 6 Rat and human B2
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Document Page 141 receptor with int
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Document Figure 9 Composition of te
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Document B. Pharmacology Figure 1 T
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Document We determined the structur
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Document Figure 3 Previously known
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Document large solvent channels and
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Document position eight from formin
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Document Table 1 Inhibition Data fo
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Document Page 166 As predicated, th
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Document References 1. Parks RE Jr.
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Document 17. Ealick SE, Rule SA, Ca
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Document 6 Structural Implications
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Document Page 176 0.43 Å) as the c
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Document Cyclotheonamide A (CtA), a
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Page 415 and 416: Document 17. Szelke M. Chemistry of
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Page 495 and 496: Document Page 398 with growth hormo
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Document Table 1 Approval Indicatio
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Document Subsequent studies have sh
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Document Cyclotheonamide A (CtA), 2
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Document D ddI, 152 tumour necrosis
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Document antistasin peptides, 281 c
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Document fragment-based programs, 5
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Document [Human immunodeficiency vi
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Document [Protease targets] serinyl
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