Purification, partial characterization, crystallization and preliminary X-ray diffraction of two cysteine-rich secretory proteins from Naja atra and Trimeresurus stejnegeri venoms.
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.
Tu
Xiongying
X
Key Laboratory of Structural Biology, Chinese Academy of Sciences, 96 Jinzhai Road, Hefei, Anhui 230026, People's Republic of China.
Wang
Jing
J
Guo
Min
M
Zheng
Dinghai
D
Teng
Maikun
M
Niu
Liwen
L
Liu
Qun
Q
Huang
Qingqiu
Q
Hao
Quan
Q
D000595:Amino Acid Sequence; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D003435:Crotalid Venoms / Q000737:chemistry* / Q000378:metabolism*; D018360:Crystallography, X-Ray; D003545:Cysteine / Q000737:chemistry*; D004546:Elapid Venoms / Q000737:chemistry*; D017815:Elapidae; D004591:Electrophoresis, Polyacrylamide Gel; D006863:Hydrogen-Ion Concentration; D008562:Membrane Glycoproteins / Q000737:chemistry*; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry; D017386:Sequence Homology, Amino Acid; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D017841:Trimeresurus; D014961:X-Ray Diffraction
D003435:Crotalid Venoms; D004546:Elapid Venoms; D008562:Membrane Glycoproteins; D010455:Peptides; C495581:natrin protein, Naja atra; C495582:stecrisp protein, Trimeresurus stejnegeri; D003545:Cysteine