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| | ==Structure of a C2 domain== | | ==Structure of a C2 domain== |
| - | <StructureSection load='3w57' size='340' side='right' caption='[[3w57]], [[Resolution|resolution]] 1.66Å' scene=''> | + | <StructureSection load='3w57' size='340' side='right'caption='[[3w57]], [[Resolution|resolution]] 1.66Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3w57]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pleuronectes_maximus Pleuronectes maximus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3W57 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3W57 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3w57]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Scophthalmus_maximus Scophthalmus maximus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3W57 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3W57 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.662Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3w56|3w56]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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 Pleuronectes maximus])</td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3w57 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w57 OCA], [https://pdbe.org/3w57 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3w57 RCSB], [https://www.ebi.ac.uk/pdbsum/3w57 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3w57 ProSAT]</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=3w57 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w57 OCA], [http://pdbe.org/3w57 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3w57 RCSB], [http://www.ebi.ac.uk/pdbsum/3w57 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3w57 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/E2FYL5_SCOMX E2FYL5_SCOMX] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Pleuronectes maximus]] | + | [[Category: Large Structures]] |
| - | [[Category: Traore, D A.K]] | + | [[Category: Scophthalmus maximus]] |
| - | [[Category: Whisstock, J C]] | + | [[Category: Traore DAK]] |
| - | [[Category: C2 domain]] | + | [[Category: Whisstock JC]] |
| - | [[Category: Lipid binding protein]]
| + | |
| Structural highlights
Function
E2FYL5_SCOMX
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ 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. Defining the interaction of perforin with calcium and the phospholipid membrane. Biochem J. 2013 Sep 27. PMID:24070258 doi:http://dx.doi.org/10.1042/BJ20130999
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