1MTN

BOVINE ALPHA-CHYMOTRYPSIN:BPTI CRYSTALLIZATION

1MTN の概要

• エントリーDOI: 10.2210/pdb1mtn/pdb
• 分子名称: ALPHA-CHYMOTRYPSIN, BASIC PANCREATIC TRYPSIN INHIBITOR, SULFATE ION, ... (6 entities in total)
• 機能のキーワード: complex, protease inhibitor, trypsin, hydrolase, serine, complex (hydrolase-inhibitor) complex, complex (hydrolase/inhibitor)
• 由来する生物種: Bos taurus (cattle); 詳細
• 細胞内の位置: Secreted, extracellular space: P00766 P00766 P00766; Secreted: P00974
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 63964.51

構造登録者

Capasso, C.,Rizzi, M.,Menegatti, E.,Ascenzi, P.,Bolognesi, M. (登録日: 1996-03-28, 公開日: 1996-08-17, 最終更新日: 2024-10-30)

主引用文献

Capasso, C.,Rizzi, M.,Menegatti, E.,Ascenzi, P.,Bolognesi, M.
Crystal structure of the bovine alpha-chymotrypsin:Kunitz inhibitor complex. An example of multiple protein:protein recognition sites.
J.Mol.Recog., 10:26-35, 1997

PubMed Abstract: The crystal structure of bovine alpha-chymotrypsin (alpha-CHT) in complex with the bovine basic pancreatic trypsin inhibitor (BPTI) has been solved and refined at 2.8 A resolution (R-factor = 0.18). The proteinase:inhibitor complex forms a compact dimer (two alpha-CHT and two BPTI molecules), which may be stabilized by surface-bound sulphate ions, in the crystalline state. Each BPTI molecule, at opposite ends, is contacting both proteinase molecules in the dimer, through the reactive site loop and through residues next to the inhibitor's C-terminal region. Specific recognition between alpha-CHT and BPTI occurs at the (re)active site interface according to structural rules inferred from the analysis of homologous serine proteinase:inhibitor complexes. Lys15, the P1 residue of BPTI, however, does not occupy the alpha-CHT S1 specificity pocket, being hydrogen bonded to backbone atoms of the enzyme surface residues Gly216 and Ser217.

PubMed: 9179777
DOI: 10.1002/(SICI)1099-1352(199701/02)10:1<26::AID-JMR351>3.0.CO;2-N

実験手法

X-RAY DIFFRACTION (2.8 Å)