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PubMed · 15159571

Purification, partial characterization, crystallization and preliminary X-ray diffraction of two cysteine-rich secretory proteins from Naja atra and Trimeresurus stejnegeri venoms.

Xiongying Tu·Jing Wang·Min Guo·Dinghai Zheng·Maikun Teng·Liwen Niu·Qun Liu·Qingqiu Huang·Quan Hao
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Abstract

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.

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Amino Acid SequenceAnimalsChromatography, High Pressure LiquidCrotalid VenomsCrystallography, X-RayCysteineElapid VenomsElapidaeElectrophoresis, Polyacrylamide GelHydrogen-Ion ConcentrationMembrane GlycoproteinsMolecular Sequence DataPeptidesSequence Homology, Amino AcidSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationTrimeresurusX-Ray DiffractionJournal ArticleResearch Support, Non-U.S. Gov't

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Xiongying Tu, Jing Wang, Min Guo, Dinghai Zheng, Maikun Teng, Liwen Niu, Qun Liu, Qingqiu Huang, Quan Hao. 2004-05-21. Purification, partial characterization, crystallization and preliminary X-ray diffraction of two cysteine-rich secretory proteins from Naja atra and Trimeresurus stejnegeri venoms.. https://doi.org/10.1107/s0907444904005670

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