4hsc
From Proteopedia
(Difference between revisions)
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4hsc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hsc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4hsc RCSB], [http://www.ebi.ac.uk/pdbsum/4hsc PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4hsc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hsc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4hsc RCSB], [http://www.ebi.ac.uk/pdbsum/4hsc PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/TACY_STRPQ TACY_STRPQ]] Sulfhydryl-activated toxin that causes cytolysis by forming pores in cholesterol containing host membranes. After binding to target membranes, the protein undergoes a major conformation change, leading to its insertion in the host membrane and formation of an oligomeric pore complex. Cholesterol may be required for binding to host membranes, membrane insertion and pore formation. Can be reversibly inactivated by oxidation (By similarity). | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 20:11, 24 December 2014
Crystal structure of a cholesterol dependent cytolysin
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