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| | ==Ral binding domain from Sec5== | | ==Ral binding domain from Sec5== |
| - | <StructureSection load='1hk6' size='340' side='right' caption='[[1hk6]], [[NMR_Ensembles_of_Models | 25 NMR models]]' scene=''> | + | <StructureSection load='1hk6' size='340' side='right'caption='[[1hk6]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1hk6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HK6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HK6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1hk6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HK6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HK6 FirstGlance]. <br> |
| - | </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=1hk6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hk6 OCA], [http://pdbe.org/1hk6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hk6 RCSB], [http://www.ebi.ac.uk/pdbsum/1hk6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1hk6 ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1hk6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hk6 OCA], [https://pdbe.org/1hk6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hk6 RCSB], [https://www.ebi.ac.uk/pdbsum/1hk6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hk6 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/EXOC2_MOUSE EXOC2_MOUSE] Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.[UniProtKB:Q96KP1] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Large Structures]] |
| - | [[Category: Camonis, J H]] | + | [[Category: Mus musculus]] |
| - | [[Category: Hopkins, L J]] | + | [[Category: Camonis JH]] |
| - | [[Category: Mirey, G]] | + | [[Category: Hopkins LJ]] |
| - | [[Category: Mott, H R]] | + | [[Category: Mirey G]] |
| - | [[Category: Nietlispach, D]] | + | [[Category: Mott HR]] |
| - | [[Category: Owen, D]] | + | [[Category: Nietlispach D]] |
| - | [[Category: Exocytosis]]
| + | [[Category: Owen D]] |
| - | [[Category: Immunoglobulin fold]]
| + | |
| - | [[Category: Ipt ral sec5 exocyst]]
| + | |
| - | [[Category: Protein transport]]
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| Structural highlights
Function
EXOC2_MOUSE Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.[UniProtKB:Q96KP1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The exocyst complex is involved in the final stages of exocytosis, when vesicles are targeted to the plasma membrane and dock. The regulation of exocytosis is vital for a number of processes, for example, cell polarity, embryogenesis, and neuronal growth formation. Regulation of the exocyst complex in mammals was recently shown to be dependent upon binding of the small G protein, Ral, to Sec5, a central component of the exocyst. This interaction is thought to be necessary for anchoring the exocyst to secretory vesicles. We have determined the structure of the Ral-binding domain of Sec5 and shown that it adopts a fold that has not been observed in a G protein effector before. This fold belongs to the immunoglobulin superfamily in a subclass known as IPT domains. We have mapped the Ral binding site on this domain and found that it overlaps with protein-protein interaction sites on other IPT domains but that it is completely different from the G protein-geranyl-geranyl interaction face of the Ig-like domain of the Rho guanine nucleotide dissociation inhibitor. This mapping, along with available site-directed mutagenesis data, allows us to predict how Ral and Sec5 may interact.
Structure of the GTPase-binding domain of Sec5 and elucidation of its Ral binding site.,Mott HR, Nietlispach D, Hopkins LJ, Mirey G, Camonis JH, Owen D J Biol Chem. 2003 May 9;278(19):17053-9. Epub 2003 Mar 6. PMID:12624092[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Mott HR, Nietlispach D, Hopkins LJ, Mirey G, Camonis JH, Owen D. Structure of the GTPase-binding domain of Sec5 and elucidation of its Ral binding site. J Biol Chem. 2003 May 9;278(19):17053-9. Epub 2003 Mar 6. PMID:12624092 doi:10.1074/jbc.M300155200
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