
Crystallization and preliminary crystallographic characterization of three peptidic inhibitors in complex with α‐thrombin
Author(s) -
Carvalho Figueiredo Ana,
Clement Cristina C.,
Philipp Manfred,
Barbosa Pereira Pedro José
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110043472
Subject(s) - thrombin , crystallization , serine protease , orthorhombic crystal system , crystallography , peptide , resolution (logic) , chemistry , protease , materials science , stereochemistry , crystal structure , biochemistry , enzyme , medicine , organic chemistry , immunology , artificial intelligence , computer science , platelet
The serine protease thrombin plays a major role in thrombosis and haemostasis. This has driven interest in thrombin inhibitors as potential antithrombotic drugs. Here, the crystallization and preliminary crystallographic analysis of human α‐thrombin in complex with three noncovalent peptide inhibitors of the general sequence d ‐Phe‐Pro‐ d ‐Arg‐P1′‐CONH 2 are reported. The crystals belonged to the orthorhombic space group P 2 1 2 1 2 1 and diffracted to beyond 1.3 Å resolution.