2ER9

X-RAY STUDIES OF ASPARTIC PROTEINASE-STATINE INHIBITOR COMPLEXES.

2ER9 の概要

• エントリーDOI: 10.2210/pdb2er9/pdb
• 関連するBIRD辞書のPRD_ID: PRD_000268
• 分子名称: ENDOTHIAPEPSIN, L363,564 (3 entities in total)
• 機能のキーワード: hydrolase-hydrolase inhibitor, acid proteinase
• 由来する生物種: Cryphonectria parasitica (chestnut blight fungus)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 34870.11

構造登録者

Cooper, J.B.,Foundling, S.I.,Boger, J.,Blundell, T.L. (登録日: 1990-10-20, 公開日: 1991-01-15, 最終更新日: 2025-03-26)

主引用文献

Cooper, J.B.,Foundling, S.I.,Blundell, T.L.,Boger, J.,Jupp, R.A.,Kay, J.
X-ray studies of aspartic proteinase-statine inhibitor complexes.
Biochemistry, 28:8596-8603, 1989

PubMed Abstract: The conformation of a statine-containing renin inhibitor complexed with the aspartic proteinase from the fungus Endothia parasitica (EC 3.4.23.6) has been determined by X-ray diffraction at 2.2-A resolution (R = 0.17). We describe the structure of the complex at high resolution and compare this with a 3.0-A resolution analysis of a bound inhibitor, L-364,099, containing a cyclohexylalanine analogue of statine. The inhibitors bind in extended conformations in the long active-site cleft, and the hydroxyl of the transition-state analogue, statine, interacts strongly with the catalytic aspartates via hydrogen bonds to the essential carboxyl groups. This work provides a detailed structural analysis of the role of statine in peptide inhibitors. It shows conclusively that statine should be considered a dipeptide analogue (occupying P1 to P1') despite lacking the equivalent of a P1' side chain, although other inhibitor residues (especially P2) may compensate by interacting at the unoccupied S1' specificity subsite.

PubMed: 2690945
DOI: 10.1021/bi00447a049

実験手法

X-RAY DIFFRACTION (2.2 Å)