4npk
From Proteopedia
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- | {{STRUCTURE_4npk| PDB=4npk | SCENE= }} | ||
- | ===Extended-Synaptotagmin 2, C2A- and C2B-domains, calcium bound=== | ||
- | {{ABSTRACT_PUBMED_24373768}} | ||
- | == | + | ==Extended-Synaptotagmin 2, C2A- and C2B-domains, calcium bound== |
- | [[http://www.uniprot.org/uniprot/ESYT2_HUMAN ESYT2_HUMAN | + | <StructureSection load='4npk' size='340' side='right'caption='[[4npk]], [[Resolution|resolution]] 2.55Å' scene=''> |
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[4npk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NPK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NPK FirstGlance]. <br> | ||
+ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.552Å</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4npk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4npk OCA], [https://pdbe.org/4npk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4npk RCSB], [https://www.ebi.ac.uk/pdbsum/4npk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4npk ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/ESYT2_HUMAN ESYT2_HUMAN] May play a role as calcium-regulated intrinsic membrane protein.<ref>PMID:17360437</ref> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Contacts between the endoplasmic reticulum and the plasma membrane involve extended synaptotagmins (E-Syts) in mammals or tricalbins in yeast, proteins with multiple C2 domains. One of the tandem C2 domains of E-Syt2 is predicted to bind Ca2+, but no Ca2+-dependent function has been attributed to this protein. We have determined the crystal structures of the tandem C2 domains of E-Syt2 in the absence and presence of Ca2+ and analyzed their Ca2+-binding properties by nuclear magnetic resonance spectroscopy. Our data reveal an unexpected V-shaped structure with a rigid orientation between the two C2 domains that is not substantially altered by Ca2+. The E-Syt2 C2A domain binds up to four Ca2+ ions, whereas the C2B domain does not bind Ca2+. These results suggest that E-Syt2 performs an as yet unidentified Ca2+-dependent function through its C2A domain and uncover fundamental differences between the properties of the tandem C2 domains of E-Syts and synaptotagmins. | ||
- | + | Structure and Ca-Binding Properties of the Tandem C Domains of E-Syt2.,Xu J, Bacaj T, Zhou A, Tomchick DR, Sudhof TC, Rizo J Structure. 2013 Dec 24. pii: S0969-2126(13)00461-9. doi:, 10.1016/j.str.2013.11.011. PMID:24373768<ref>PMID:24373768</ref> | |
- | + | ||
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | < | + | </div> |
- | + | <div class="pdbe-citations 4npk" style="background-color:#fffaf0;"></div> | |
- | + | ||
- | [[ | + | ==See Also== |
- | [[ | + | *[[Synaptotagmin|Synaptotagmin]] |
- | + | *[[Synaptotagmin 3D structures|Synaptotagmin 3D structures]] | |
- | [[Category: | + | == References == |
- | [[Category: | + | <references/> |
- | [[Category: | + | __TOC__ |
- | [[Category: | + | </StructureSection> |
- | [[Category: | + | [[Category: Homo sapiens]] |
+ | [[Category: Large Structures]] | ||
+ | [[Category: Rizo J]] | ||
+ | [[Category: Tomchick DR]] | ||
+ | [[Category: Xu J]] |
Current revision
Extended-Synaptotagmin 2, C2A- and C2B-domains, calcium bound
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