Lysin
From Proteopedia
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<StructureSection load='1lis' size='340' side='right' caption='Abalone lysin (PDB code [[1lis]])' scene='60/607850/Lysin_fertilization_protein/1'> | <StructureSection load='1lis' size='340' side='right' caption='Abalone lysin (PDB code [[1lis]])' scene='60/607850/Lysin_fertilization_protein/1'> | ||
== Function == | == Function == | ||
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== Structural highlights == | == Structural highlights == | ||
| - | The structure of lysin, refined at 1.9 angstroms resolution, reveals an alpha-helical, amphipathic molecule<scene name='60/607850/Alpha_helixes/1'>To see alpha helixes press here</scene>. you can see the alpha helixes in pink. <scene name='60/607850/Surface/1'>the surface of the protein</scene> exhibits three features: two tracks of basic residues that span the length of the molecule, a solvent-exposed cluster of <scene name='60/607850/Aromatic_and_aliphatic/1'>aromatic and aliphatic amino acids</scene>,(in green) and an extended amino-terminal hypervariable domain that is species-specific. The structure suggests possible mechanisms of action<ref>PMID: | + | The structure of lysin, refined at 1.9 angstroms resolution, reveals an alpha-helical, amphipathic molecule<scene name='60/607850/Alpha_helixes/1'>To see alpha helixes press here</scene>. you can see the alpha helixes in pink. <scene name='60/607850/Surface/1'>the surface of the protein</scene> exhibits three features: two tracks of basic residues that span the length of the molecule, a solvent-exposed cluster of <scene name='60/607850/Aromatic_and_aliphatic/1'>aromatic and aliphatic amino acids</scene>,(in green) and an extended amino-terminal hypervariable domain that is species-specific. The structure suggests possible mechanisms of action<ref>PMID:8266073</ref>. |
Revision as of 11:24, 31 January 2016
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References
- ↑ Shaw A, McRee DE, Vacquier VD, Stout CD. The crystal structure of lysin, a fertilization protein. Science. 1993 Dec 17;262(5141):1864-7. PMID:8266073
Proteopedia Page Contributors and Editors (what is this?)
Michal Harel, Carmit Ginesin, Alexander Berchansky, Joel L. Sussman, Jaime Prilusky
