4CAA

CLEAVED ANTICHYMOTRYPSIN T345R

「1CT3」から置き換えられました

4CAA の概要

• エントリーDOI: 10.2210/pdb4caa/pdb
• 分子名称: ANTICHYMOTRYPSIN (2 entities in total)
• 機能のキーワード: serpin, serine protease inhibitor, antichymotrypsin
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Secreted: P01011 P01011
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 42941.27

構造登録者

Lukacs, C.M.,Christianson, D.W. (登録日: 1997-08-14, 公開日: 1998-02-25, 最終更新日: 2024-05-22)

主引用文献

Lukacs, C.M.,Rubin, H.,Christianson, D.W.
Engineering an anion-binding cavity in antichymotrypsin modulates the "spring-loaded" serpin-protease interaction.
Biochemistry, 37:3297-3304, 1998

PubMed Abstract: Expressed in a kinetically trapped folding state, a serpin couples the thermodynamic driving force of a massive beta-sheet rearrangement to the inhibition of a target protease. Hence, the serpin-protease interaction is the premier example of a "spring-loaded" protein-protein interaction. Amino acid substitutions in the hinge region of a serpin reactive loop can weaken the molecular spring, which converts the serpin from an inhibitor into a substrate. To probe the molecular basis of this conversion, we report the crystal structure of A349R antichymotrypsin in the reactive loop cleaved state at 2.1 A resolution. This amino acid substitution does not block the beta-sheet rearrangement despite the burial of R349 in the hydrophobic core of the cleaved serpin along with a salt-linked acetate ion. The inhibitory activity of this serpin variant is not obliterated; remarkably, its inhibitory properties are anion-dependent due to the creation of an anion-binding cavity in the cleaved serpin.

PubMed: 9521649
DOI: 10.1021/bi972359e

実験手法

X-RAY DIFFRACTION (2.9 Å)