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1lxd

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Current revision (08:28, 10 April 2024) (edit) (undo)
 
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<StructureSection load='1lxd' size='340' side='right'caption='[[1lxd]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='1lxd' size='340' side='right'caption='[[1lxd]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1lxd]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LXD OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1LXD FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1lxd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LXD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LXD FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RALGDS C-TERMINAL DOMAIN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1lxd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lxd OCA], [http://pdbe.org/1lxd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1lxd RCSB], [http://www.ebi.ac.uk/pdbsum/1lxd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1lxd ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1lxd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lxd OCA], [https://pdbe.org/1lxd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lxd RCSB], [https://www.ebi.ac.uk/pdbsum/1lxd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lxd ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/GNDS_RAT GNDS_RAT]] 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.
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[https://www.uniprot.org/uniprot/GNDS_RAT GNDS_RAT] 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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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/main_output.php?pdb_ID=1lxd ConSurf].
</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=1lxd ConSurf].
<div style="clear:both"></div>
<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 Ras-interacting domains of the the protein-kinase Raf and the Ral guanine nucleotide dissociation stimulator, RalGDS, lack extensive sequence similarity, but their overall three-dimensional structures are very similar to each other. Mutational analysis indicated that three residues in the RalGDS domain are critical for its interaction with Ras.
 
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Three-dimensional structure of the Ras-interacting domain of RalGDS.,Huang L, Weng X, Hofer F, Martin GS, Kim SH Nat Struct Biol. 1997 Aug;4(8):609-15. PMID:9253406<ref>PMID:9253406</ref>
 
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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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<div class="pdbe-citations 1lxd" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Buffalo rat]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Hofer, F]]
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[[Category: Rattus norvegicus]]
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[[Category: Huang, L]]
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[[Category: Hofer F]]
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[[Category: Kim, S H]]
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[[Category: Huang L]]
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[[Category: Martin, G S]]
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[[Category: Kim SH]]
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[[Category: Weng, X W]]
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[[Category: Martin GS]]
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[[Category: Cdc25 family]]
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[[Category: Weng XW]]
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[[Category: Cross-talk]]
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[[Category: Phosphorylation]]
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[[Category: Ralgd]]
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[[Category: Ras binding]]
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[[Category: Signal transduction]]
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[[Category: Ubiquitin fold]]
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Current revision

CRYSTAL STRUCTURE OF THE RAS INTERACTING DOMAIN OF RALGDS, A GUANINE NUCLEOTIDE DISSOCIATION STIMULATOR OF RAL PROTEIN

PDB ID 1lxd

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