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| | ==Structure of the Ca2+-bound Rabphilin 3A C2B domain SNAP25 complex (P21 space group)== | | ==Structure of the Ca2+-bound Rabphilin 3A C2B domain SNAP25 complex (P21 space group)== |
| - | <StructureSection load='5low' size='340' side='right' caption='[[5low]], [[Resolution|resolution]] 2.80Å' scene=''> | + | <StructureSection load='5low' size='340' side='right'caption='[[5low]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5low]] is a 14 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LOW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LOW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5low]] is a 14 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LOW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LOW FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 2.8Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Rph3a ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat]), Snap25, Snap ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</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>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=5low FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5low OCA], [http://pdbe.org/5low PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5low RCSB], [http://www.ebi.ac.uk/pdbsum/5low PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5low ProSAT]</span></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=5low FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5low OCA], [https://pdbe.org/5low PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5low RCSB], [https://www.ebi.ac.uk/pdbsum/5low PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5low ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/RP3A_RAT RP3A_RAT]] Protein transport. Probably involved with Ras-related protein Rab-3A in synaptic vesicle traffic and/or synaptic vesicle fusion. Could play a role in neurotransmitter release by regulating membrane flow in the nerve terminal. [[http://www.uniprot.org/uniprot/SNP25_RAT SNP25_RAT]] t-SNARE involved in the molecular regulation of neurotransmitter release. May play an important role in the synaptic function of specific neuronal systems. Associates with proteins involved in vesicle docking and membrane fusion. Regulates plasma membrane recycling through its interaction with CENPF. | + | [https://www.uniprot.org/uniprot/RP3A_RAT RP3A_RAT] Protein transport. Probably involved with Ras-related protein Rab-3A in synaptic vesicle traffic and/or synaptic vesicle fusion. Could play a role in neurotransmitter release by regulating membrane flow in the nerve terminal. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 5low" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5low" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Exophilin 3D structures|Exophilin 3D structures]] |
| | + | *[[Rabphilin|Rabphilin]] |
| | + | *[[Synaptosomal-associated protein|Synaptosomal-associated protein]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Buffalo rat]] | + | [[Category: Large Structures]] |
| - | [[Category: Ferrer-Orta, C]] | + | [[Category: Rattus norvegicus]] |
| - | [[Category: Verdaguer, N]] | + | [[Category: Ferrer-Orta C]] |
| - | [[Category: C2 domain]] | + | [[Category: Verdaguer N]] |
| - | [[Category: Calcium]]
| + | |
| - | [[Category: Exocytosis]]
| + | |
| - | [[Category: Membrane fusion]]
| + | |
| Structural highlights
Function
RP3A_RAT Protein transport. Probably involved with Ras-related protein Rab-3A in synaptic vesicle traffic and/or synaptic vesicle fusion. Could play a role in neurotransmitter release by regulating membrane flow in the nerve terminal.
Publication Abstract from PubMed
Membrane fusion is essential in a myriad of eukaryotic cell biological processes, including the synaptic transmission. Rabphilin-3A is a membrane trafficking protein involved in the calcium-dependent regulation of secretory vesicle exocytosis in neurons and neuroendocrine cells, but the underlying mechanism remains poorly understood. Here, we report the crystal structures and biochemical analyses of Rabphilin-3A C2B-SNAP25 and C2B-phosphatidylinositol 4,5-bisphosphate (PIP2) complexes, revealing how Rabphilin-3A C2 domains operate in cooperation with PIP2/Ca(2+) and SNAP25 to bind the plasma membrane, adopting a conformation compatible to interact with the complete SNARE complex. Comparisons with the synaptotagmin1-SNARE show that both proteins contact the same SNAP25 surface, but Rabphilin-3A uses a unique structural element. Data obtained here suggest a model to explain the Ca(2+)-dependent fusion process by membrane bending with a myriad of variations depending on the properties of the C2 domain-bearing protein, shedding light to understand the fine-tuning control of the different vesicle fusion events.
Structural characterization of the Rabphilin-3A-SNAP25 interaction.,Ferrer-Orta C, Perez-Sanchez MD, Coronado-Parra T, Silva C, Lopez-Martinez D, Baltanas-Copado J, Gomez-Fernandez JC, Corbalan-Garcia S, Verdaguer N Proc Natl Acad Sci U S A. 2017 Jul 3;114(27):E5343-E5351. doi:, 10.1073/pnas.1702542114. Epub 2017 Jun 20. PMID:28634303[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ferrer-Orta C, Perez-Sanchez MD, Coronado-Parra T, Silva C, Lopez-Martinez D, Baltanas-Copado J, Gomez-Fernandez JC, Corbalan-Garcia S, Verdaguer N. Structural characterization of the Rabphilin-3A-SNAP25 interaction. Proc Natl Acad Sci U S A. 2017 Jul 3;114(27):E5343-E5351. doi:, 10.1073/pnas.1702542114. Epub 2017 Jun 20. PMID:28634303 doi:http://dx.doi.org/10.1073/pnas.1702542114
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