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3m3r
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=3m3r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m3r OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3m3r RCSB], [http://www.ebi.ac.uk/pdbsum/3m3r 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=3m3r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m3r OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3m3r RCSB], [http://www.ebi.ac.uk/pdbsum/3m3r PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/HLA_STAAU HLA_STAAU]] Alpha-toxin binds to the membrane of eukaryotic cells resulting in the release of low-molecular weight molecules and leading to an eventual osmotic lysis. Heptamer oligomerization and pore formation is required for lytic activity. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 13:58, 24 December 2014
Crystal structure of the M113F alpha-hemolysin mutant complexed with beta-cyclodextrin
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