3vwi
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=3vwi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vwi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vwi RCSB], [http://www.ebi.ac.uk/pdbsum/3vwi 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=3vwi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vwi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vwi RCSB], [http://www.ebi.ac.uk/pdbsum/3vwi 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 22:01, 25 December 2014
High resolution crystal structure of FraC in the monomeric form
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