3w56
From Proteopedia
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| - | + | ==Structure of a C2 domain== | |
| - | === | + | <StructureSection load='3w56' size='340' side='right' caption='[[3w56]], [[Resolution|resolution]] 1.60Å' scene=''> |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[3w56]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Psemx Psemx]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3W56 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3W56 FirstGlance]. <br> | ||
| + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">C2P1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=52904 PSEMX])</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=3w56 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w56 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3w56 RCSB], [http://www.ebi.ac.uk/pdbsum/3w56 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Following its secretion from cytotoxic lymphocytes into the immune synapse, perforin binds to target cell membranes through its Ca2+-dependent C2 domain. Membrane-bound perforin then forms pores that allow passage of pro-apoptopic granzymes into the target cell. Here, structural and biochemical studies reveal that Ca2+ binding triggers a conformational change in the C2 domain that permits four key hydrophobic residues to interact with the plasma membrane. However, contrary to previous suggestions, these movements and membrane binding do not trigger irreversible conformational changes in the pore-forming MACPF domain, indicating that subsequent monomer-monomer interactions at the membrane surface are required for perforin pore formation. | ||
| - | + | Defining the interaction of perforin with calcium and the phospholipid membrane.,Traore DA, Brennan AJ, Law RH, Dogovski C, Perugini MA, Lukoyanova N, Leung EW, Norton RS, Lopez JA, Browne KA, Yagita H, Lloyd GJ, Ciccone A, Verschoor S, Trapani JA, Whisstock JC, Voskoboinik I Biochem J. 2013 Sep 27. PMID:24070258<ref>PMID:24070258</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Psemx]] | [[Category: Psemx]] | ||
| - | [[Category: Traore, D A.K | + | [[Category: Traore, D A.K]] |
| - | [[Category: Whisstock, J C | + | [[Category: Whisstock, J C]] |
[[Category: C2 domain]] | [[Category: C2 domain]] | ||
[[Category: Lipid binding protein]] | [[Category: Lipid binding protein]] | ||
Revision as of 09:07, 4 January 2015
Structure of a C2 domain
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