1CGJ

THREE-DIMENSIONAL STRUCTURE OF THE COMPLEXES BETWEEN BOVINE CHYMOTRYPSINOGEN*A AND TWO RECOMBINANT VARIANTS OF HUMAN PANCREATIC SECRETORY TRYPSIN INHIBITOR (KAZAL-TYPE)

1CGJ の概要

• エントリーDOI: 10.2210/pdb1cgj/pdb
• 分子名称: ALPHA-CHYMOTRYPSINOGEN, PANCREATIC SECRETORY TRYPSIN INHIBITOR (KAZAL TYPE) VARIANT 4 (3 entities in total)
• 機能のキーワード: serine protease-inhibitor complex, serine protease-inhibitor complex complex, serine protease/inhibitor complex
• 由来する生物種: Bos taurus (cattle); 詳細
• 細胞内の位置: Secreted, extracellular space: P00766; Secreted: P00995
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 31983.12

構造登録者

Hecht, H.J.,Szardenings, M.,Collins, J.,Schomburg, D. (登録日: 1991-10-08, 公開日: 1993-10-31, 最終更新日: 2024-10-30)

主引用文献

Hecht, H.J.,Szardenings, M.,Collins, J.,Schomburg, D.
Three-dimensional structure of the complexes between bovine chymotrypsinogen A and two recombinant variants of human pancreatic secretory trypsin inhibitor (Kazal-type).
J.Mol.Biol., 220:711-722, 1991

PubMed Abstract: 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.

PubMed: 1870127
DOI: 10.1016/0022-2836(91)90112-J

実験手法

X-RAY DIFFRACTION (2.3 Å)