4npk: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==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 [http://en.wikipedia.org/wiki/Human Human]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NPK FirstGlance]. <br> | |||
==Function== | </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> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4npj|4npj]]</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4npk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4npk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4npk RCSB], [http://www.ebi.ac.uk/pdbsum/4npk 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> | [[http://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> | |||
[[Category: Rizo, J | == References == | ||
[[Category: Tomchick, D R | <references/> | ||
[[Category: Xu, J | __TOC__ | ||
</StructureSection> | |||
[[Category: Human]] | |||
[[Category: Rizo, J]] | |||
[[Category: Tomchick, D R]] | |||
[[Category: Xu, J]] | |||
[[Category: C2 domain]] | [[Category: C2 domain]] | ||
[[Category: Calcium/phospholipid binding protein]] | [[Category: Calcium/phospholipid binding protein]] | ||
Revision as of 16:25, 25 December 2014
Extended-Synaptotagmin 2, C2A- and C2B-domains, calcium boundExtended-Synaptotagmin 2, C2A- and C2B-domains, calcium bound
Structural highlights
Function[ESYT2_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. References
|
| ||||||||||||||||||||