4npj: Difference between revisions

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 ==Extended-Synaptotagmin 2, C2A- and C2B-domains==
-<StructureSection load='4npj' size='340' side='right' caption='[[4npj]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
+<StructureSection load='4npj' size='340' side='right'caption='[[4npj]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4npj]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NPJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NPJ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4npj]] is a 2 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=4NPJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NPJ FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 2.101&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4npk|4npk]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ESYT2, extended-synaptotagmin 2, FAM62B, KIAA1228 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4npj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4npj OCA], [https://pdbe.org/4npj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4npj RCSB], [https://www.ebi.ac.uk/pdbsum/4npj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4npj 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=4npj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4npj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4npj RCSB], [http://www.ebi.ac.uk/pdbsum/4npj PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/ESYT2_HUMAN ESYT2_HUMAN]] May play a role as calcium-regulated intrinsic membrane protein.<ref>PMID:17360437</ref>
+[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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+==See Also==
-</div>
+*[[Synaptotagmin 3D structures|Synaptotagmin 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
-[[Category: Rizo, J]]
+[[Category: Large Structures]]
-[[Category: Tomchick, D R]]
+[[Category: Rizo J]]
-[[Category: Xu, J]]
+[[Category: Tomchick DR]]
-[[Category: C2 domain]]
+[[Category: Xu J]]
-[[Category: Calcium/phospholipid binding protein]]
-[[Category: Er to plasma membrane]]
-[[Category: Membrane protein]]
-[[Category: Membrane traffic]]
-[[Category: Plasma membrane]]
-[[Category: Protein targeting]]