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Document ascorbate synthesis, by a genetically modified Erwinia herbicola. Science 1985; 230:144–149. Page 246 39. El-Kabbani O, Green NC, Lin G, Carson M, Narayanam SVL, Moore K, Flynn TG, DeLucas LJ. Structures of human and porcine aldehyde reductase: an enzyme implicated in diabetic complications. Acta Crystallogr D 1994; 50:859–868. 40. El-Kabbani O, Judge K, Ginell SL, Myles Daa, DeLucas LJ, Flynn TG. Structure of porcine aldehyde reductase holoenzyme. Nat Struct Biol 1995; 2:687–692. 41. Wilson DK, Nakano T, Petrash JM, Quiocho FA. 1.7 Å structure of FR-1, a fibroblast growth factorinduced member of the aldo-keto reductase family complexed with coenzyme and inhibitor. Biochemistry 1995; 34:14323–14330. 42. Hoog SS, Pawlowski JE, Alzari PM, Penning TM, Lewis M. Three-dimensional structure of rat liver 3α-hydroxysteroid/dihydrodiol dehydrogenase: a member of the aldo-keto reductase superfamily. Proc Natl Acad Sci USA 1994; 91:2517–2521. 43 Schoichet B, Bodian D, Kuntz I. Molecular docking using shape descriptors. J Comp Chem 1992; 13:380–397. 44 Straatsma TP, McCammon JA. Computational alchemy. Annu Rev Phys Chem 1992 43:407–435. 45 Allen FG, Bellar SA, Brice MD, Cartwright BA, Doubleday A, Higgs H, Hummelink T, Hummelink- Peters BG, Kennard O, Motherwell WDS, Rodgeres JR, Watson DG. The Cambridge Crystallographic Data Centre: Computer based search retrieval, analysis and display of information. Acta Crystallogr B35:2331–2339. 46 Shen C, Sigman DS. New inhibitors of aldose reductase: anti-oximes of aromatic aldehydes. Arch Biochem Biophys 1991; 286:596–603. 47 Mylari BL, Beyer TA, Scott PJ, Aldinger CE, Dee MF, Siegel TW, Zembrowski WJ. Potent, orally active aldose reductase inhbitors related to zopolrestat: surrogates for benzothiazole side chain. J Med Chem 1992; 35:457–465. 48 Kraulis PJ. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J Appl Crystallog 1991; 24:946–950. 49 Nicholls A, Sharp KA, Honig B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 1991; 11:281–296. http://legacy.netlibrary.com/nlreader/nlReader.dll?bookid=12640&filename=Page_246.html [4/5/2004 5:10:07 PM]
Document 10 Structure-Based Design of Thrombin Inhibitors Patricia C. Weber and Michael Czarniecki Schering-Plough Research Institute, Kenilworth, New Jersey I. Roles of Thrombin in Hemostasis and the Therapeutic Utility of Thrombin Inhibitors Page 247 Thrombin is a serine protease that plays critical roles in both blood clot formation and anticoagulation. In the penultimate step of the coagulation cascade, thrombin cleaves soluble fibrinogen to form insoluble fibrin. Thrombin also activates other coagulation factors including Factor XIII, the enzyme responsible for crosslinking fibrin to further stabilize the thrombus. Additional clot-promoting functions include stimulation of platelet aggregation by cleavage of the thrombin receptor. In contrast to its roles in clot formation, thrombin participates in anticoagulant functions. For example, thrombin-mediated activation of protein C, a protease involved in anticoagulation, is enhanced when thrombin is complexed with thrombomodulin, and in this complex, thrombin can neither cleave fibrinogen nor activate platelets. The interrelationship among thrombin's many roles in hemostasis is complex and presents several mechanisms for inhibition of thrombus formation. For recent reviews see References 1 through 5. Most drug discovery efforts focus on thrombin inhibition as a means to prevent the serious consequences of thrombus formation in myocardial infarction and stroke. Thrombin inhibitors may also prevent clot formation in patients prone to deep vein thrombosis or repeat heart attack. In combination with thrombus dissolution therapies, thrombin inhibitors may decrease the incidence of reocclusion due, in part, to the release of active clot-bound thrombin. In this article, recent examples of small molecule inhibitors interacting at the fibrinogen primary specificity pocket and with residues of the catalytic triad http://legacy.netlibrary.com/nlreader/nlReader.dll?bookid=12640&filename=Page_247.html [4/5/2004 5:10:09 PM]
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