1xx5
From Proteopedia
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. 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 Page seeded by OCA on Sat May 3 15:37:00 2008
Categories: Naja atra | Single protein | Guo, M. | Lou, X H. | Niu, L W. | Shen, B. | Teng, M K. | Wang, J. | Crisp | Natrin
