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4e82
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=4e82 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e82 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4e82 RCSB], [http://www.ebi.ac.uk/pdbsum/4e82 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=4e82 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e82 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4e82 RCSB], [http://www.ebi.ac.uk/pdbsum/4e82 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/DEF5_HUMAN DEF5_HUMAN]] Has antimicrobial activity against Gram-negative and Gram-positive bacteria. Defensins are thought to kill microbes by permeabilizing their plasma membrane. All DEFA5 peptides exert antimicrobial activities, but their potency is affected by peptide processing.<ref>PMID:12021776</ref> <ref>PMID:15616305</ref> <ref>PMID:17088326</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Revision as of 08:52, 24 December 2014
Crystal structure of monomeric variant of human alpha-defensin 5, HD5 (Glu21EMe mutant)
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