1OS0

Thermolysin with an alpha-amino phosphinic inhibitor

「1NO0」から置き換えられました

1OS0 の概要

• エントリーDOI: 10.2210/pdb1os0/pdb
• 関連するPDBエントリー: 1KEI 1QF0 1QF1 1QF2 1TLP 2TMN
• 分子名称: Thermolysin, ZINC ION, CALCIUM ION, ... (6 entities in total)
• 機能のキーワード: thermolysin, alpha-amino phosphinic compound, neprylisin, hydrolase, metal-binding, metalloprotease, protease, secreted, zymogen, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• 由来する生物種: Bacillus thermoproteolyticus
• 細胞内の位置: Secreted: P00800
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 35160.68

構造登録者

Selkti, M.,Tomas, A.,Prange, T. (登録日: 2003-03-18, 公開日: 2003-03-25, 最終更新日: 2023-08-16)

主引用文献

Selkti, M.,Tomas, A.,Gaucher, J.F.,Prange, T.,Fournie-Zaluski, M.C.,Chen, H.,Roques, B.P.
Interactions of a new alpha-aminophosphinic derivative inside the active site of TLN (thermolysin): a model for zinc-metalloendopeptidase inhibition.
Acta Crystallogr.,Sect.D, 59:1200-1205, 2003

PubMed Abstract: A new alpha-aminophosphinic compound able to inhibit both zinc-containing exopeptidases and endopeptidases has been crystallized with TLN as a model in order to investigate the mode of zinc recognition by the phosphinic moiety and to evaluate the potential role of the free alpha-amino group in the formation of enzyme-inhibitor complexes. In addition to the main interactions between the backbone of the inhibitor and the enzyme active site, it is observed that the phosphinic group acts as a distorted bidentate ligand for the zinc ion, while the free alpha-amino function does not directly participate in interactions within the active site. Association of the present data and the K(i) values of various analogues of the inhibitor towards TLN and neprilysin suggests differences in the hydrophobicity of the S(1)-S(2) domains of the enzymes. This could be taken into account in the design of selective inhibitors.

PubMed: 12832763
DOI: 10.1107/S0907444903010060

実験手法

X-RAY DIFFRACTION (2.1 Å)