The crystal structure of lysin, a fertilization protein.
The crystal structure of lysin, a fertilization protein.
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受精蛋白赖氨酸的晶体结构。
DOI：
10.1126/science.8266073
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发表时间：
1993
期刊：
影响因子：
--
通讯作者：
Stout,CD
中科院分区：
文献类型：
--
作者：
Shaw,A;McRee,DE;Vacquier,VD;Stout,CD
溶素是鲍鱼精子中的一种蛋白质，它在卵子的包膜上形成一个洞，使精子能够穿过包膜与卵子融合。在1.9埃分辨率下精修的溶素结构显示出一种α-螺旋的两亲分子。蛋白质的表面表现出三个特征：跨越分子长度的两个碱性残基轨道，暴露于溶剂的芳香族和脂肪族氨基酸簇，以及具有物种特异性的延伸氨基末端高变结构域。该结构表明可能的作用机制。
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 α-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.