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Papers In Press, published online ahead of print December 13, 2004
Department of Molecular and Cell Biology, School of Life Sciences, Hefei, Anhui 230026
Corresponding Author: lwniu{at}ustc.edu.cn
Stecrisp from Trimeresurus stejnegeri snake venom belongs to a family of cysteine-rich secretory proteins (CRISP)1, which have various functions related to the sperm-egg fusion, innate host defense and blockage of ion channels. Here we present the crystal structure of stecrisp refined to 1.6 Å resolution. It shows stecrisp contains 3 regions: a PR-1 (pathogenesis-related proteins of group1) domain, a hinge and a cysteine-rich domain (CRD). Similar conformation of solvent exposed and conserved residues (His60, Glu75, Glu96, His115) in PR-1 domain with their counterparts in homologous structures suggests they may share some molecular mechanism. Three flexible loops of hyper-variable sequence surrounding the possible substrate binding site in PR-1 domain show evident difference in homologous structures, implying that a great diversity of species specific and substrate specific interactions may be involved in recognition and catalysis. The hinge is fixed by two crossed disulfide bonds formed by four out of ten characteristic cysteines in the C-terminal region, and is important to stabilize the N-terminal PR-1 domain. Spatially separated from the PR-1 domain, CRD possesses a similar fold with two K+-channel inhibitors (Bgk, Shk). Several candidates for the possible functional sites of ion channel blocking are located in a solvent exposed loop in CRD. The structure of stecrisp will provide a prototypic architecture for structural and functional exploration of the diverse members of the CRISP family.
J. Biol. Chem, 10.1074/jbc.M413566200
Submitted on December 2, 2004
Revised on December 10, 2004
Accepted on December 13, 2004
Crystal structure of cysteine-rich secretory protein stecrisp reveals the cysteine-rich domain has a K+-channel inhibitor-like fold
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