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- W2595286528 abstract "The crystal structure of a doubleheadeda-chymotrypsin inhibitor, WCI, from wingedbean seeds has now been refined at 2.3A°resolutionto an R-factor of 18.7% for 9,897 reflections. Thecrystals belong to the hexagonal space group P6122with cell parameters a 5 b 5 61.8A°and c 5 212.8A°.The final model has a good stereochemistry and aroot mean square deviation of 0.011A°and 1.14° fromideality for bond length and bond angles, respectively.A total of 109 ordered solvent molecules werelocalized in the structure. This improved structureat 2.3A°led to an understanding of themechanism ofinhibition of the protein against a-chymotrypsin.Ananalysis of this higher resolution structure alsohelped us to predict the location of the secondreactive site of the protein, about which no previousbiochemical information was available. The inhibitorstructure is spherical and has twelve antiparallelb-strands with connecting loops arrangedin a characteristic b-trefoil fold common to otherhomologous serine protease inhibitors in the Kunitz(STI) family as well as to some non homologousfunctionally unrelated proteins. Awide variation inthe surface loop regions is seen in the latter ones.Proteins 1999;35:321–331. r 1999Wiley-Liss, Inc." @default.
- W2595286528 created "2017-03-23" @default.
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- W2595286528 date "1999-01-01" @default.
- W2595286528 modified "2023-09-24" @default.
- W2595286528 title "Refined Crystal Structure (2.3A°) of a Double-HeadedWinged Bean a-Chymotrypsin Inhibitor and Locationof Its Second Reactive Site" @default.
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