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THREE-DIMENSIONAL STRUCTURE OF THE COMPLEXES BETWEEN BOVINE CHYMOTRYPSINOGEN*A AND TWO RECOMBINANT VARIANTS OF HUMAN PANCREATIC SECRETORY TRYPSIN INHIBITOR (KAZAL-TYPE)
OverviewOverview
Variants of the human pancreatic secretory trypsin inhibitor (PSTI) have, been created during a protein design project to generate a high-affinity, inhibitor with respect to some serine proteases other than trypsin. Two, modified versions of human PSTI with high affinity for chymotrypsin were, crystallized as a complex with chymotrypsinogen. Both crystallize, isomorphously in space group P4(1)2(1)2 with lattice constants a = 84.4 A, c = 86.7 A and diffract to 2.3 A resolution. The structure was solved by, molecular replacement. The final R-value after refinement with 8.0 to 2.3, A resolution data was 19.5% for both complexes after inclusion of about 50, bound water molecules. The overall three-dimensional structure of PSTI is, similar to the structure of porcine PSTI in the trypsinogen complex, (1TGS). Small differences in the relative orientation of the binding loop, and the core of the inhibitors indicate flexible adaptation to the, proteases. The chymotrypsinogen part of the complex is similar to, chymotrypsin. After refolding induced by binding of the inhibitor the, root-mean-square difference of the active site residues A186 to A195 and, A217 to A222 compared to chymotrypsin was 0.26 A.
About this StructureAbout this Structure
1CGI is a Protein complex structure of sequences from Bos taurus and Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Three-dimensional structure of the complexes between bovine chymotrypsinogen A and two recombinant variants of human pancreatic secretory trypsin inhibitor (Kazal-type)., Hecht HJ, Szardenings M, Collins J, Schomburg D, J Mol Biol. 1991 Aug 5;220(3):711-22. PMID:1870127
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