1PSO

The crystal structure of human pepsin and its complex with pepstatin

1PSO の概要

• エントリーDOI: 10.2210/pdb1pso/pdb
• 関連するBIRD辞書のPRD_ID: PRD_000557
• 分子名称: PEPSIN 3A, PEPSTATIN (3 entities in total)
• 機能のキーワード: acid proteinase, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Secreted: P00790
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 35317.78

構造登録者

Fujinaga, M.,Chernaia, M.M.,Tarasova, N.,Mosimann, S.C.,James, M.N.G. (登録日: 1995-01-23, 公開日: 1995-04-20, 最終更新日: 2024-10-09)

主引用文献

Fujinaga, M.,Chernaia, M.M.,Tarasova, N.I.,Mosimann, S.C.,James, M.N.
Crystal structure of human pepsin and its complex with pepstatin.
Protein Sci., 4:960-972, 1995

PubMed Abstract: The three-dimensional crystal structure of human pepsin and that of its complex with pepstatin have been solved by X-ray crystallographic methods. The native pepsin structure has been refined with data collected to 2.2 A resolution to an R-factor of 19.7%. The pepsin:pepstatin structure has been refined with data to 2.0 A resolution to an R-factor of 18.5%. The hydrogen bonding interactions and the conformation adopted by pepstatin are very similar to those found in complexes of pepstatin with other aspartic proteinases. The enzyme undergoes a conformational change upon inhibitor binding to enclose the inhibitor more tightly. The analysis of the binding sites indicates that they form an extended tube without distinct binding pockets. By comparing the residues on the binding surface with those of the other human aspartic proteinases, it has been possible to rationalize some of the experimental data concerning the different specificities. At the S1 site, valine at position 120 in renin instead of isoleucine, as in the other enzymes, allows for binding of larger hydrophobic residues. The possibility of multiple conformations for the P2 residue makes the analysis of the S2 site difficult. However, it is possible to see that the specific interactions that renin makes with histidine at P2 would not be possible in the case of the other enzymes. At the S3 site, the smaller volume that is accessible in pepsin compared to the other enzymes is consistent with its preference for smaller residues at the P3 position.

PubMed: 7663352

実験手法

X-RAY DIFFRACTION (2 Å)