6o6h

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (14:50, 13 March 2024) (edit) (undo)
 
Line 3: Line 3:
<StructureSection load='6o6h' size='340' side='right'caption='[[6o6h]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
<StructureSection load='6o6h' size='340' side='right'caption='[[6o6h]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[6o6h]] is a 1 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=6O6H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6O6H FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[6o6h]] is a 1 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=6O6H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6O6H FirstGlance]. <br>
-
</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>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#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=6o6h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6o6h OCA], [https://pdbe.org/6o6h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6o6h RCSB], [https://www.ebi.ac.uk/pdbsum/6o6h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6o6h 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=6o6h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6o6h OCA], [https://pdbe.org/6o6h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6o6h RCSB], [https://www.ebi.ac.uk/pdbsum/6o6h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6o6h ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[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).
+
[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).
-
<div style="background-color:#fffaf0;">
+
-
== Publication Abstract from PubMed ==
+
-
Integrin activation controls cell adhesion, migration, invasion, and extracellular matrix remodeling. RIAM (RAP1-GTP-interacting adaptor molecule) is recruited by activated RAP1 to the plasma membrane (PM) to mediate integrin activation via an inside-out signaling pathway. This process requires the association of the pleckstrin homology (PH) domain of RIAM with the membrane PIP2. We identify a conserved intermolecular interface that masks the PIP2-binding site in the PH domains of RIAM. Our data indicate that phosphorylation of RIAM by Src family kinases disrupts this PH-mediated interface, unmasks the membrane PIP2-binding site, and promotes integrin activation. We further demonstrate that this process requires phosphorylation of Tyr267 and Tyr427 in the RIAM PH domain by Src. Our data reveal an unorthodox regulatory mechanism of small GTPase effector proteins by phosphorylation-dependent PM association of the PH domain and provide new insights into the link between Src kinases and integrin signaling.
+
-
 
+
-
Phosphorylation of RIAM by Src Promotes Integrin Activation by Unmasking the PH Domain of RIAM.,Cho EA, Zhang P, Kumar V, Kavalchuk M, Zhang H, Huang Q, Duncan JS, Wu J Structure. 2020 Nov 27. pii: S0969-2126(20)30423-8. doi:, 10.1016/j.str.2020.11.011. PMID:33275877<ref>PMID:33275877</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 6o6h" style="background-color:#fffaf0;"></div>
+
-
== References ==
+
-
<references/>
+
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Lk3 transgenic mice]]
+
[[Category: Mus musculus]]
-
[[Category: Wu, J]]
+
[[Category: Wu J]]
-
[[Category: Rap1 effector ra-ph]]
+
-
[[Category: Signaling protein]]
+

Current revision

RIAM cc-RA-PH structure in the P21212 space group

PDB ID 6o6h

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools