View source for 2rgf


==RBD OF RAL GUANOSINE-NUCLEOTIDE EXCHANGE FACTOR (PROTEIN), NMR, 10 STRUCTURES==
<StructureSection load='2rgf' size='340' side='right'caption='[[2rgf]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2rgf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RGF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RGF FirstGlance]. <br>
</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=2rgf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rgf OCA], [https://pdbe.org/2rgf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rgf RCSB], [https://www.ebi.ac.uk/pdbsum/2rgf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rgf ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GNDS_HUMAN GNDS_HUMAN] Stimulates the dissociation of GDP from the Ras-related RalA and RalB GTPases which allows GTP binding and activation of the GTPases. Interacts and acts as an effector molecule for R-Ras, H-Ras, K-Ras, and Rap.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rg/2rgf_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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/main_output.php?pdb_ID=2rgf ConSurf].
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== Publication Abstract from PubMed ==
The solution structure of the Ras-binding domain (RBD) of Ral guanine-nucleotide exchange factor RalGEF was solved by NMR spectroscopy. The overall structure is similar to that of Raf-RBD, another effector of Ras, although the sequence identity is only 13%. 15N chemical shifts changes in the complex of RalGEF-RBD with Ras indicate an interaction similar to the intermolecular beta-sheet observed for the complex between Ras and Raf-RBD.

Structure of the Ras-binding domain of RalGEF and implications for Ras binding and signalling.,Geyer M, Herrmann C, Wohlgemuth S, Wittinghofer A, Kalbitzer HR Nat Struct Biol. 1997 Sep;4(9):694-9. PMID:9302994<ref>PMID:9302994</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 2rgf" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Geyer M]]
[[Category: Herrmann C]]
[[Category: Kalbitzer HR]]
[[Category: Wittinghofer A]]