View source for 4jgw


==The conformation of a docking site for SH3 domains is pre-selected in the Guanine Nucleotide Exchange Factor Rlf==
<StructureSection load='4jgw' size='340' side='right'caption='[[4jgw]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4jgw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JGW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JGW FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</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=4jgw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jgw OCA], [https://pdbe.org/4jgw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jgw RCSB], [https://www.ebi.ac.uk/pdbsum/4jgw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jgw ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RGL2_MOUSE RGL2_MOUSE] Probable guanine nucleotide exchange factor. Putative effector of Ras and/or Rap. Associates with the GTP-bound form of Rap 1A and H-Ras in vitro.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Rlf is a guanine nucleotide exchange factor for the small G-proteins RalA and RalB and couples Ras- to Ral-signalling. Here the crystal structure of the catalytic module of Rlf consisting of a REM- and a CDC25-homology domain is determined. The structure is distinguished by an extended three stranded beta-sheet called the flagpole. The flagpole is a conserved element in the RalGDS family of guanine nucleotide exchange factors and stabilises the orientation of the REM-domain relative to the CDC25-homology domain. A proline-rich sequence in the flagpole is unique to Rlf and several proteins that interact with this sequence by SH3 domains are identified. Conformational pre-selection results in a gain of affinity and contributes to the establishment of SH3 domain selectivity.

The guanine nucleotide exchange factor Rlf interacts with SH3 domain-containing proteins via a binding site with a preselected conformation.,Popovic M, Jakobi AJ, Rensen-de Leeuw M, Rehmann H J Struct Biol. 2013 Sep;183(3):312-9. doi: 10.1016/j.jsb.2013.07.009. Epub 2013, Jul 24. PMID:23891840<ref>PMID:23891840</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4jgw" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Jakobi AJ]]
[[Category: Popovic M]]
[[Category: Rehmann H]]