1QLP

2.0 ANGSTROM STRUCTURE OF INTACT ALPHA-1-ANTITRYPSIN: A CANONICAL TEMPLATE FOR ACTIVE SERPINS

「2PSI」から置き換えられました

1QLP の概要

• エントリーDOI: 10.2210/pdb1qlp/pdb
• 関連するPDBエントリー: 1ATU 1KCT 1PSI 2PSI 7API 8API 9API
• 分子名称: ALPHA-1-ANTITRYPSIN (2 entities in total)
• 機能のキーワード: serine protease inhibitor, serpin, glycoprotein, polymorphism, emphysema, disease mutation, acute phase
• 由来する生物種: HOMO SAPIENS (HUMAN)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 44380.44

構造登録者

Elliott, P.R.,Pei, X.Y.,Dafforn, T.,Read, R.J.,Carrell, R.W.,Lomas, D.A. (登録日: 1999-09-10, 公開日: 1999-09-27, 最終更新日: 2023-12-13)

主引用文献

Elliott, P.R.,Pei, X.Y.,Dafforn, T.R.,Lomas, D.A.
Topography of a 2.0 A structure of alpha1-antitrypsin reveals targets for rational drug design to prevent conformational disease.
Protein Sci., 9:1274-1281, 2000

PubMed Abstract: Members of the serpin family of serine proteinase inhibitors play important roles in the inflammatory, coagulation, fibrinolytic, and complement cascades. An inherent part of their function is the ability to undergo a structural rearrangement, the stressed (S) to relaxed (R) transition, in which an extra strand is inserted into the central A beta-sheet. In order for this transition to take place, the A sheet has to be unusually flexible. Malfunctions in this flexibility can lead to aberrant protein linkage, serpin inactivation, and diseases as diverse as cirrhosis, thrombosis, angioedema, emphysema, and dementia. The development of agents that control this conformational rearrangement requires a high resolution structure of an active serpin. We present here the topology of the archetypal serpin alpha1-antitrypsin to 2 A resolution. This structure allows us to define five cavities that are potential targets for rational drug design to develop agents that will prevent conformational transitions and ameliorate the associated disease.

PubMed: 10933492
DOI: 10.1110/ps.9.7.1274

実験手法

X-RAY DIFFRACTION (2 Å)