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Crevice‐forming mutants in the rigid core of bovine pancreatic trypsin inhibitor: Crystal structures of F22A, Y23A, N43G, and F45A
Author(s) -
Danishefsky Avis T.,
Housset Dominique,
Wlodawer Alexander,
Kim KeySun,
Tao Feng,
Fuchs James,
Woodward Clare
Publication year - 1993
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560020409
Subject(s) - mutant , trypsin , trypsin inhibitor , molecule , chemistry , crystal structure , crystallography , core (optical fiber) , protein structure , small molecule , wild type , biochemistry , enzyme , materials science , gene , organic chemistry , composite material
Crystal structures of four mutants of bovine pancreatic trypsin inhibitor (F22A, Y23A, N43G, and F45A), engineered to alter their stability properties, have been determined. The mutated residues, which are highly conserved among Kunitz‐type inhibitors, are located in the rigid core of the molecule. Replacement of the partially buried bulky residues of the wild‐type protein with smaller residues resulted in crevices open to the exterior of the molecule. The overall three‐dimensional structure of these mutants is very similar to that of the wild‐type protein and only small rearrangements are observed among the atoms lining the crevices.