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Crystallization and preliminary crystallographic characterization of three peptidic inhibitors in complex with ?-thrombin.

ABSTRACT: 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 ?-thrombin in complex with three noncovalent peptide inhibitors of the general sequence D-Phe-Pro-D-Arg-P1'-CONH2 are reported. The crystals belonged to the orthorhombic space group P2(1)2(1)2(1) and diffracted to beyond 1.3?Å resolution.

SUBMITTER: Carvalho Figueiredo A

PROVIDER: S-EPMC3079972 | biostudies-literature | 2011 Jan

REPOSITORIES: biostudies-literature

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Crystallization and preliminary crystallographic characterization of three peptidic inhibitors in complex with α-thrombin.

Carvalho Figueiredo Ana A Clement Cristina C CC Philipp Manfred M Barbosa Pereira Pedro José PJ

Acta crystallographica. Section F, Structural biology and crystallization communications 20101221 Pt 1

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'-CONH2 are reported. The crystals belonged to the orthorhombic space group P2(1)2(1)2(1) and diffracted to beyond 1.3 Å resolution. ...[more]

PMID: 21206024

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