3qxl

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Current revision (10:50, 21 February 2024) (edit) (undo)
 
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<StructureSection load='3qxl' size='340' side='right'caption='[[3qxl]], [[Resolution|resolution]] 2.24&Aring;' scene=''>
<StructureSection load='3qxl' size='340' side='right'caption='[[3qxl]], [[Resolution|resolution]] 2.24&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3qxl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QXL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QXL FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3qxl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QXL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QXL FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RALGPS1, KIAA0351, RALGEF2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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]] 2.237&#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=3qxl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qxl OCA], [https://pdbe.org/3qxl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qxl RCSB], [https://www.ebi.ac.uk/pdbsum/3qxl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qxl ProSAT]</span></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=3qxl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qxl OCA], [https://pdbe.org/3qxl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qxl RCSB], [https://www.ebi.ac.uk/pdbsum/3qxl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qxl ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/RGPS1_HUMAN RGPS1_HUMAN]] Guanine nucleotide exchange factor (GEF) for the small GTPase RALA. May be involved in cytoskeletal organization (By similarity). Guanine nucleotide exchange factor for.<ref>PMID:10747847</ref> <ref>PMID:10889189</ref>
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[https://www.uniprot.org/uniprot/RGPS1_HUMAN RGPS1_HUMAN] Guanine nucleotide exchange factor (GEF) for the small GTPase RALA. May be involved in cytoskeletal organization (By similarity). Guanine nucleotide exchange factor for.<ref>PMID:10747847</ref> <ref>PMID:10889189</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The guanine-nucleotide exchange factor (GEF) RalGPS1a activates small GTPase Ral proteins such as RalA and RalB by stimulating the exchange of Ral bound GDP to GTP, thus regulating various downstream cellular processes. RalGPS1a is composed of an N-terminal Cdc25-like catalytic domain, followed by a PXXP motif and a C-terminal pleckstrin homology (PH) domain. The Cdc25 domain of RalGPS1a, which shares about 30% sequence identity with other Cdc25-domain proteins, is thought to be directly engaged in binding and activating the substrate Ral protein. Here we report the crystal structure of the Cdc25 domain of RalGPS1a. The bowl shaped structure is homologous to the Cdc25 domains of SOS and RasGRF1. The most remarkable difference between these three Cdc25 domains lies in their active sites, referred to as the helical hairpin region. Consistent with previous enzymological studies, the helical hairpin of RalGPS1a adopts a conformation favorable for substrate binding. A modeled RalGPS1a-RalA complex structure reveals an extensive binding surface similar to that of the SOS-Ras complex. However, analysis of the electrostatic surface potential suggests an interaction mode between the RalGPS1a active site helical hairpin and the switch 1 region of substrate RalA distinct from that of the SOS-Ras complex.
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Structural study of the Cdc25 domain from Ral-specific guanine-nucleotide exchange factor RalGPS1a.,Peng W, Xu J, Guan X, Sun Y, Zhang XC, Li X, Rao Z Protein Cell. 2011 Apr 14. PMID:21494904<ref>PMID:21494904</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 3qxl" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Guan, X]]
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[[Category: Guan X]]
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[[Category: Li, X]]
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[[Category: Li X]]
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[[Category: Peng, W]]
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[[Category: Peng W]]
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[[Category: Rao, Z]]
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[[Category: Rao Z]]
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[[Category: Sun, Y]]
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[[Category: Sun Y]]
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[[Category: Xu, J]]
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[[Category: Xu J]]
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[[Category: Zhang, X C]]
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[[Category: Zhang XC]]
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[[Category: Cdc25 domain homology]]
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[[Category: Guanine-nucleotide exchange factor]]
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[[Category: Signaling protein]]
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[[Category: Small gtpase ral subfamily]]
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Current revision

Crystal structure of the CDC25 Domain from Ral-specific Guanine-nucleotide Exchange Factor RalGPS1a

PDB ID 3qxl

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OCA

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