3zwj
From Proteopedia
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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=3zwj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zwj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3zwj RCSB], [http://www.ebi.ac.uk/pdbsum/3zwj 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=3zwj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zwj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3zwj RCSB], [http://www.ebi.ac.uk/pdbsum/3zwj PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/ACTPC_ACTFR ACTPC_ACTFR]] Pore-forming protein that forms cations-selective hydrophilic pores of around 1 nm and causes cardiac stimulation and hemolysis. Pore formation is a multi-step process that involves specific recognition of membrane sphingomyelin (but neither cholesterol nor phosphatidylcholine) using aromatic rich region and adjacent phosphocholine (POC) binding site, firm binding to the membrane (mainly driven by hydrophobic interactions) accompanied by the transfer of the N-terminal region to the lipid-water interface and finally pore formation after oligomerization of several monomers.<ref>PMID:19563820</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Revision as of 21:47, 24 December 2014
CRYSTAL STRUCTURE OF THE PORE-FORMING TOXIN FRAC FROM ACTINIA FRAGACEA (Form 3)
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