3tca

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Current revision (13:23, 14 March 2024) (edit) (undo)
 
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<StructureSection load='3tca' size='340' side='right'caption='[[3tca]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
<StructureSection load='3tca' size='340' side='right'caption='[[3tca]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3tca]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TCA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TCA FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3tca]] 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=3TCA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TCA FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Apbb1ip, Prel1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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]] 2.35&#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=3tca FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tca OCA], [https://pdbe.org/3tca PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tca RCSB], [https://www.ebi.ac.uk/pdbsum/3tca PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tca 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=3tca FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tca OCA], [https://pdbe.org/3tca PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tca RCSB], [https://www.ebi.ac.uk/pdbsum/3tca PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tca ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/AB1IP_MOUSE AB1IP_MOUSE]] Appears to function in the signal transduction from Ras activation to actin cytoskeletal remodeling. Suppresses insulin-induced promoter activities through AP1 and SRE. Mediates Rap1-induced adhesion (By similarity).
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[https://www.uniprot.org/uniprot/AB1IP_MOUSE AB1IP_MOUSE] Appears to function in the signal transduction from Ras activation to actin cytoskeletal remodeling. Suppresses insulin-induced promoter activities through AP1 and SRE. Mediates Rap1-induced adhesion (By similarity).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Adaptive immunity depends on lymphocyte adhesion that is mediated by the integrin lymphocyte functional antigen 1 (LFA-1). The small guanosine triphosphatase Rap1 regulates LFA-1 adhesiveness through one of its effectors, Rap1-interacting adapter molecule (RIAM). We show that RIAM was recruited to the lymphocyte plasma membrane (PM) through its Ras association (RA) and pleckstrin homology (PH) domains, both of which were required for lymphocyte adhesion. The N terminus of RIAM inhibited membrane translocation. In vitro, the RA domain bound both Rap1 and H-Ras with equal but relatively low affinity, whereas in vivo only Rap1 was required for PM association. The PH domain bound phosphoinositol 4,5-bisphosphate (PI(4,5)P(2)) and was responsible for the spatial distribution of RIAM only at the PM of activated T cells. We determined the crystal structure of the RA and PH domains and found that, despite an intervening linker of 50 aa, the two domains were integrated into a single structural unit, which was critical for proper localization to the PM. Thus, the RA-PH domains of RIAM function as a proximity detector for activated Rap1 and PI(4,5)P(2).
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Rap1-interacting adapter molecule (RIAM) associates with the plasma membrane via a proximity detector.,Wynne JP, Wu J, Su W, Mor A, Patsoukis N, Boussiotis VA, Hubbard SR, Philips MR J Cell Biol. 2012 Oct 15;199(2):317-29. doi: 10.1083/jcb.201201157. Epub 2012 Oct, 8. PMID:23045549<ref>PMID:23045549</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 3tca" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Lk3 transgenic mice]]
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[[Category: Mus musculus]]
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[[Category: Hubbard, S R]]
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[[Category: Hubbard SR]]
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[[Category: Wu, J]]
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[[Category: Wu J]]
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[[Category: Integrin signaling]]
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[[Category: Ph domain]]
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[[Category: Ra domain]]
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[[Category: Rap1-interacting adaptor molecule]]
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[[Category: Rbd]]
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[[Category: Signaling protein]]
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Current revision

Crystal structure of the Ras-associating and pleckstrin-homology domains of RIAM

PDB ID 3tca

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Proteopedia Page Contributors and Editors (what is this?)

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