1xx5

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(New page: 200px<br /><applet load="1xx5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xx5, resolution 2.40&Aring;" /> '''Crystal Structure of...)
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Revision as of 04:16, 21 November 2007

Image:1xx5.gif

1xx5, resolution 2.40Å

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Crystal Structure of Natrin from Naja atra snake venom

Overview

Cysteine-rich secretory proteins (CRISPs) are widely distributed in, mammals and snake venoms. They possess apparent homology but varying, functions. The structure of CRISPs has remained elusive. Two novel members, of the family, natrin and stecrisp, have been purified from Naja atra and, Trimeresurus stejnegeri venoms, respectively. Their crystals diffract, X-rays to resolution limits of 2.1 and 1.6 angstroms, respectively, and, belong to the orthorhombic system with different space groups, unit-cell, parameters and numbers of molecules per asymmetric unit. Their structures, will contribute a structural basis for further functional studies of this, family.

About this Structure

1XX5 is a Single protein structure of sequence from Naja atra with EOH as ligand. Full crystallographic information is available from OCA.

Reference

Purification, partial characterization, crystallization and preliminary X-ray diffraction of two cysteine-rich secretory proteins from Naja atra and Trimeresurus stejnegeri venoms., Tu X, Wang J, Guo M, Zheng D, Teng M, Niu L, Liu Q, Huang Q, Hao Q, Acta Crystallogr D Biol Crystallogr. 2004 Jun;60(Pt 6):1108-11. Epub 2004, May 21. PMID:15159571

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