4npk: Difference between revisions
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==Extended-Synaptotagmin 2, C2A- and C2B-domains, calcium bound== | |||
<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]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Rizo J]] | |||
[[Category: Tomchick DR]] | |||
[[Category: Xu J]] | |||
Latest revision as of 20:01, 20 September 2023
Extended-Synaptotagmin 2, C2A- and C2B-domains, calcium boundExtended-Synaptotagmin 2, C2A- and C2B-domains, calcium bound
Structural highlights
FunctionESYT2_HUMAN May play a role as calcium-regulated intrinsic membrane protein.[1] Publication Abstract from PubMedContacts 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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