THE CRYSTAL-STRUCTURE OF LYSIN, A FERTILIZATION PROTEIN

被引：54

作者：

SHAW, A

MCREE, DE

VACQUIER, VD

STOUT, CD

机构：

[1] SCRIPPS RES INST, DEPT MOLEC BIOL, LA JOLLA, CA 92037 USA

[2] UNIV CALIF SAN DIEGO, SCRIPPS INST OCEANOG, CTR MARINE BIOMED & BIOTECHNOL, LA JOLLA, CA 92093 USA

来源：

SCIENCE | 1993年 / 262卷 / 5141期

关键词：

D O I：

10.1126/science.8266073

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Lysin, a protein from abalone sperm, creates a hole in the envelope of the egg, permitting the sperm to pass through the envelope and fuse with the egg. The structure of lysin, refined at 1.9 angstroms resolution, reveals an alpha-helical, amphipathic molecule. The surface of the protein exhibits three features: two tracks of basic residues that span the length of the molecule, a solvent-exposed cluster of aromatic and aliphatic amino acids, and an extended amino-terminal hypervariable domain that is species-specific. The structure suggests possible mechanisms of action.

引用

页码：1864 / 1867

页数：4

共 18 条

[1]

BAGINSKY ML, 1990, J BIOL CHEM, V265, P4958

[2] CRYSTALLOGRAPHIC REFINEMENT BY SIMULATED ANNEALING - APPLICATION TO CRAMBIN [J].