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Document Figure 4 Extended binding modes for substrates and inhibitors. Sites in the enzyme (S) and in the inhibitor (P) are designated <strong>by</strong> the Schecter-Berger notation [48]. http://legacy.netlibrary.com/nlreader/nlReader.dll?bookid=12640&filename=Page_270.html (2 of 2) [4/5/2004 5:12:45 PM]
Document Table 3 Active Site Sequences for Factor Xa Substrates and Inhibitors Substrates P4 P3 P2 P1 P'1 P'2 P'3 P'4 PT 271,272 Ile Glu Gly Arg Thr Ala Thr Ser PT 320,321 Ile Asp Gly Arg Ile Val Glu Gly FVII Pro Gln Gly Arg Ile Val Gly Gly FV Lys Lys Tyr Arg Ser Leu His Leu Inhibitors Antistasin Val Arg Cys Arg Val His Cys Pro Ecotin Val Ser Thr Met Met Ala Cys Pro TFPI-II Gly Ile Cys Arg Gly Tyr Ile Thr AcAP5 Cys Arg Ser Arg Gly Cys Leu Leu AcAP6 Cys Arg Ser Phe Ser Cys Pro Gly Page 271 inhibitors [42]. A potent inhibitor of both Factor VIIa and Xa as well as trypsin, TFPI does not, however, have significant activity against leukocyte elastase, urokinase, activated Protein C, tissue factor plasminogen activator, thrombin, or kallikrein [53,54]. The second Kunitz domain from the Nterminus of TFPI has been identified as primarily responsible for the Factor Xa inhibition while both the first and second domains contribute to inhibition of Factor VIIa [42] (Figure 5). The proposed mechanism for this Factor-Xa-dependent inhibition of FVIIa/tissue factor involves the formation of a quarternary FXa-TFPI-FVIIa/TF complex [42]. The recombinant, isolated second domain, TFPI-II, has a K i for Factor Xa of 90 nM [50] compared to 3 pM [49] for the intact protein. The sequence of the P4–P5' region of the Factor Xa inhibitory second Kunitz domain (Table 3) has been incorporated into a prototypic Kunitz inhibitor, bovine pancreatic inhibitor (BPTI), to produce potent and selective Factor Xa inhibitors [75,76]. B. Antistasin (ATS) Antistasin is one of several anticoagulants isolated from the Mexican leech, Haementeria officinalis [14]. It is a 119-amino-acid cysteine-rich protein with a primary structure that shows a two-fold sequence symmetry suggesting the molecule possesses two separate and distinct domains [51]. Mutagenesis studies have shown that ATS binds to Factor Xa in a substratelike manner in the P3(Arg 32–P'3(Cys 37) regions and is cleaved only in the first domain [55]. http://legacy.netlibrary.com/nlreader/nlReader.dll?bookid=12640&filename=Page_271.html (1 of 2) [4/5/2004 5:12:47 PM]
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Structure-based Drug Design 14 Stru
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Document dine) and didanosine (dide
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Document 4 Bradykinin Receptor Anta
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Document We determined the structur
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Document Table 1 Inhibition Data fo
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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 All effects of the IL-1 fa
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Document 17 Structure and Functiona
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Document Table 1 Approval Indicatio
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Document Page 438 proteins. One pot
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Document Page 443 that allowed for
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Document Figure 5 Velcro-key model
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Document Figure 6 Proposed receptor
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Document Page 462 strains of influe
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Document Page 476 nM, respectively.
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Document VI. Conclusion Page 480 It
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Document 21. Both GW, Sleigh MJ, Co
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Document A. The Canyon Page 491 The
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Document Subsequent studies have sh
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Document Page 495 of the RNA and pr
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Document Figure 5 Some compounds wh
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Document Page 629 ML, Clare M, Decr
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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 antagonistic activity, 416
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Document Kininogen, 119 high molecu
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Document Matrix-metalloproteinase (
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Document RT inhibitor, 41, 56 Nonpe
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Document Phosphoglycerate kinase (P
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Document [Protease targets] serinyl
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