5h4y
From Proteopedia
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== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/SYT5_HUMAN SYT5_HUMAN] May be involved in Ca(2+)-dependent exocytosis of secretory vesicles through Ca(2+) and phospholipid binding to the C2 domain or may serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis. Regulates the Ca(2+)-dependent secretion of norepinephrine in PC12 cells. Required for export from the endocytic recycling compartment to the cell surface (By similarity). | [https://www.uniprot.org/uniprot/SYT5_HUMAN SYT5_HUMAN] May be involved in Ca(2+)-dependent exocytosis of secretory vesicles through Ca(2+) and phospholipid binding to the C2 domain or may serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis. Regulates the Ca(2+)-dependent secretion of norepinephrine in PC12 cells. Required for export from the endocytic recycling compartment to the cell surface (By similarity). | ||
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| - | == Publication Abstract from PubMed == | ||
| - | Synaptotagmins constitute a family of multifunctional integral membrane proteins found predominantly on vesicles in neural and endocrine tissues. 17 isoforms of synaptotagmin family in mammals have been identified, 7 isoforms among them are known to be able to bind Ca2+ via their C2 domains. This study presents the crystal structure of the first C2 domain (C2A domain) of synaptotagmin 5 complexed with Ca2+ at 1.90A resolution. Comparison of the Ca2+-binding pocket of synaptotagmin 5 C2A domain with other synaptotagmin C2 domains demonstrated that a serine residue locating at Ca2+-binding loop probably responsible to the conformational variation of Ca2+-binding pocket, and thus impacts the Ca2+-binding mechanism of C2 domain, which is verified by structural analysis of the serine mutant and Ca2+-binding assays via isothermal titration calorimetry. Alteration of Ca2+-binding mechanism might be correlated with different Ca2+ response rates of synaptotagmins, which is the basis of the functions of synaptotagmins in regulating various types of Ca2+-triggered vesicle-membrane fusion processes. | ||
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| - | Structural analysis of Ca2+-binding pocket of synaptotagmin 5 C2A domain.,Qiu X, Ge J, Gao Y, Teng M, Niu L Int J Biol Macromol. 2016 Oct 25. pii: S0141-8130(16)32153-5. doi:, 10.1016/j.ijbiomac.2016.10.083. PMID:27793683<ref>PMID:27793683</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 5h4y" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Synaptotagmin 3D structures|Synaptotagmin 3D structures]] | *[[Synaptotagmin 3D structures|Synaptotagmin 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Crystal structure of human synaptotagmin 5 C2A domain
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Categories: Homo sapiens | Large Structures | Gao Y | Niu L | Qiu X | Teng M
