The Crystal Structure of Lysin, a Fertilization Protein
pmid: 8266073
The Crystal Structure of Lysin, a Fertilization Protein
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.
- University of California, San Diego United States
- University of California, San Diego United States
- Scripps Institution of Oceanography United States
- Scripps Research Institute United States
Models, Molecular, Molecular Sequence Data, Crystallography, X-Ray, Protein Structure, Secondary, Mucoproteins, Mollusca, Computer Graphics, Animals, Amino Acid Sequence, Vitelline Membrane
Models, Molecular, Molecular Sequence Data, Crystallography, X-Ray, Protein Structure, Secondary, Mucoproteins, Mollusca, Computer Graphics, Animals, Amino Acid Sequence, Vitelline Membrane
9 Research products, page 1 of 1
- 2016IsRelatedTo
- 2017IsRelatedTo
- 1993IsSupplementTo
- 1993IsRelatedTo
citations This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).59 popularity This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.Average influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).Top 10% impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.Top 10%
