1MCT

THE REFINED 1.6 ANGSTROMS RESOLUTION CRYSTAL STRUCTURE OF THE COMPLEX FORMED BETWEEN PORCINE BETA-TRYPSIN AND MCTI-A, A TRYPSIN INHIBITOR OF SQUASH FAMILY

1MCT の概要

• エントリーDOI: 10.2210/pdb1mct/pdb
• 分子名称: BETA-TRYPSIN, TRYPSIN INHIBITOR A, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: hydrolase-hydrolase inhibitor complex, proteinase, hydrolase/hydrolase inhibitor
• 由来する生物種: Sus scrofa (pig); 詳細
• 細胞内の位置: Secreted, extracellular space: P00761; Secreted: P30709
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 26695.43

構造登録者

Huang, Q.,Liu, S.,Tang, Y. (登録日: 1992-10-24, 公開日: 1994-01-31, 最終更新日: 2024-10-30)

主引用文献

Huang, Q.,Liu, S.,Tang, Y.
Refined 1.6 A resolution crystal structure of the complex formed between porcine beta-trypsin and MCTI-A, a trypsin inhibitor of the squash family. Detailed comparison with bovine beta-trypsin and its complex.
J.Mol.Biol., 229:1022-1036, 1993

PubMed Abstract: The crystal structure of the complex formed by porcine beta-trypsin with the MCTI-A inhibitor (Momordica charantia, Linn. Cucurbitaceae) has been determined at 1.6 A resolution using the molecular replacement method. The sequence of MCTI-A was determined by recognizing the electron density, and shows that MCTI-A is a member of the squash family of trypsin inhibitors. We report the first high-resolution structure of porcine beta-trypsin. Detailed comparisons have been made on the overall structure, solvent structure and active-site geometries between this complex and bovine beta-trypsin and its complexes. On the basis of our results, we discuss the interaction patterns between inhibitor and trypsin. Unlike other complex structures formed by bovine trypsin with inhibitors, no out-of-plane distortion around the inhibitor's scissible peptide was observed. The role of the trypsin catalytic triad is also discussed on the basis of this structure.

PubMed: 8445634
DOI: 10.1006/jmbi.1993.1102

実験手法

X-RAY DIFFRACTION (1.6 Å)