1rlf

<StructureSection load='1rlf' size='340' side='right'caption='[[1rlf]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1rlf]] is a 1 chain structure with sequence from [https://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=1RLF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RLF FirstGlance]. <br>

</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=1rlf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rlf OCA], [https://pdbe.org/1rlf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rlf RCSB], [https://www.ebi.ac.uk/pdbsum/1rlf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rlf ProSAT]</span></td></tr>

[[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.

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== Publication Abstract from PubMed ==

Ral-specific guanine nucleotide exchange factors RalGDS, Rgl, and Rlf have been suggested to function as intermediates between Ras and Ral pathways by being able to bind Ras proteins through their C-terminal Ras-binding domains (RBD). The RBDs of RalGDS and of the Ser/Thr kinase c-Raf-1 have been shown to have the same tertiary structure. In contrast to the RBDs of Raf and RalGDS, which bind either Ras or Rap with high affinity, Rlf-RBD has a similar affinity for both GTP-binding proteins. To be able to compare these RBDs on a structural level, we have solved the three-dimensional structure of Rlf-RBD by NMR spectroscopy. The overall tertiary structure of Rlf-RBD shows the betabetaalphabetabetaalphabeta-fold of the ubiquitin superfamily and is very similar to that of RalGDS-RBD. The binding interface of Rlf-RBD to Ras was mapped using chemical shift analysis and indicated a binding mode similar to that in the case of Rap.Raf-RBD. However, comparison of the putatively interacting regions revealed structural differences which are proposed to be responsible for the different substrate affinities of Rlf-, RalGDS-, and Raf-RBD.

Structure determination of the Ras-binding domain of the Ral-specific guanine nucleotide exchange factor Rlf.,Esser D, Bauer B, Wolthuis RM, Wittinghofer A, Cool RH, Bayer P Biochemistry. 1998 Sep 29;37(39):13453-62. PMID:9753431<ref>PMID:9753431</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Lk3 transgenic mice]]

[[Category: Bauer, B]]

[[Category: Bay, P]]

[[Category: Cool, R H]]

[[Category: Esser, D]]

[[Category: Wittinghofer, A]]

[[Category: Wolthuis, R M.F]]

[[Category: Signal transduction protein]]