1ELC

Analogous inhibitors of elastase do not always bind analogously

1ELC の概要

• エントリーDOI: 10.2210/pdb1elc/pdb
• 関連するPDBエントリー: 1ELA 1ELB
• 関連するBIRD辞書のPRD_ID: PRD_000367
• 分子名称: ELASTASE, 6-ammonio-N-(trifluoroacetyl)-L-norleucyl-N-[4-(1-methylethyl)phenyl]-L-phenylalaninamide, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: hydrolase-hydrolase inhibitor complex, serine proteinase, hydrolase/hydrolase inhibitor
• 由来する生物種: Sus scrofa (pig)
• 細胞内の位置: Secreted: P00772
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 26475.68

構造登録者

Mattos, C.,Rasmussen, B.,Ding, X.,Petsko, G.A.,Ringe, D. (登録日: 1993-12-07, 公開日: 1994-04-30, 最終更新日: 2024-11-20)

主引用文献

Mattos, C.,Rasmussen, B.,Ding, X.,Petsko, G.A.,Ringe, D.
Analogous inhibitors of elastase do not always bind analogously.
Nat.Struct.Biol., 1:55-58, 1994

PubMed Abstract: It has been assumed that the structure of a single inhibitor complex is sufficient to define the available subsites of an enzyme that has a unique binding site and a uniquely defined mode for ligand binding--the specificity for these subsites can thus be probed by kinetic experiments. Elastase is an enzyme for which these traditional assumptions, which underlie such structural and kinetic studies, do not hold. Three new crystal structures of elastase complexed to chemically similar inhibitors with similar binding affinities reveal a diversity of binding modes as well as two new subsites on elastase. The existence of multiple binding sites and different binding modes for such similar inhibitors indicates that researchers must proceed with caution when using kinetics to map out protein subsites.

PubMed: 7656008
DOI: 10.1038/nsb0194-55

実験手法

X-RAY DIFFRACTION (1.75 Å)