Science · 1993 · 55 citations · 15 references
Life SciencesBiochemistryMolecular BiologyMolecular BiophysicsProtein BiochemistryStructural BiologyEgg ProteinsFertilization BiologyProtein DomainsProtein StructureSperm BiologyStructural DomainsAmino AcidsAmphipathic Helical PeptidesAmphipathic PeptidesCrystal Structure RefinementEgg Envelope ProteinsFusion Proteins In FertilizationMolecular Mechanisms Of FertilizationSperm-egg Recognition
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.
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Solvent-Accessible Surfaces of Proteins and Nucleic Acids
Michael L. Connolly · Science · 1983 · 2.7K citations