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1hk6

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[[Image:1hk6.png|left|200px]]
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==RAL BINDING DOMAIN FROM SEC5==
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<StructureSection load='1hk6' size='340' side='right' caption='[[1hk6]], [[NMR_Ensembles_of_Models | 25 NMR models]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1hk6]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HK6 FirstGlance]. <br>
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</td></tr><tr><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://www.rcsb.org/pdb/explore.do?structureId=1hk6 RCSB], [http://www.ebi.ac.uk/pdbsum/1hk6 PDBsum]</span></td></tr>
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<table>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hk/1hk6_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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{{STRUCTURE_1hk6| PDB=1hk6 | SCENE= }}
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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<ref>PMID:12624092</ref>
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===RAL BINDING DOMAIN FROM SEC5===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_12624092}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[1hk6]] is a 1 chain structure with sequence from [http://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].
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:012624092</ref><references group="xtra"/>
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Camonis, J H.]]
[[Category: Camonis, J H.]]

Revision as of 08:30, 28 September 2014

RAL BINDING DOMAIN FROM SEC5

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