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Crystallization and preliminary crystallographic characterization of the N-terminal Kunitz domain of boophilin.

ABSTRACT: Boophilin is a tight-binding thrombin inhibitor composed of two canonical Kunitz-type domains in a tandem arrangement. Thrombin-bound boophilin can inhibit a second trypsin-like serine proteinase, most likely through the reactive loop of its N-terminal Kunitz domain. Here, the crystallization and preliminary crystallographic analysis of the isolated N-terminal domain of boophilin is reported. The crystals belonged to the orthorhombic space group P2(1)2(1)2(1) and diffracted to beyond 1.8 Å resolution using a sealed-tube home source and to 0.87 Å resolution at a synchrotron source.

SUBMITTER: Cereija TB

PROVIDER: S-EPMC3325814 | biostudies-literature | 2012 Apr

REPOSITORIES: biostudies-literature

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Crystallization and preliminary crystallographic characterization of the N-terminal Kunitz domain of boophilin.

Cereija Tatiana B TB Figueiredo Ana C AC de Sanctis Daniele D Tanaka Aparecida S AS Pereira Pedro José Barbosa PJ

Acta crystallographica. Section F, Structural biology and crystallization communications 20120327 Pt 4

Boophilin is a tight-binding thrombin inhibitor composed of two canonical Kunitz-type domains in a tandem arrangement. Thrombin-bound boophilin can inhibit a second trypsin-like serine proteinase, most likely through the reactive loop of its N-terminal Kunitz domain. Here, the crystallization and preliminary crystallographic analysis of the isolated N-terminal domain of boophilin is reported. The crystals belonged to the orthorhombic space group P2(1)2(1)2(1) and diffracted to beyond 1.8 Å resol ...[more]

PMID: 22505414

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