5fr1: Difference between revisions
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<StructureSection load='5fr1' size='340' side='right'caption='[[5fr1]], [[Resolution|resolution]] 2.75Å' scene=''> | <StructureSection load='5fr1' size='340' side='right'caption='[[5fr1]], [[Resolution|resolution]] 2.75Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5fr1]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5fr1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FR1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FR1 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.75Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ALY:N(6)-ACETYLLYSINE'>ALY</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=5fr1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fr1 OCA], [https://pdbe.org/5fr1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fr1 RCSB], [https://www.ebi.ac.uk/pdbsum/5fr1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fr1 ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/GDIR1_BOVIN GDIR1_BOVIN] In glioma cells, inhibits cell migration and invasion by mediating the signals of SEMA5A and PLXNB3 that lead to inactivation of RAC1 (By similarity). Regulates the GDP/GTP exchange reaction of the Rho proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them.<ref>PMID:2120668</ref> <ref>PMID:9194563</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
*[[Rho GTPase|Rho GTPase]] | *[[Guanine nucleotide dissociation inhibitor|Guanine nucleotide dissociation inhibitor]] | ||
*[[Rho GTPase 3D structures|Rho GTPase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Bos taurus]] | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Kuhlmann | [[Category: Kuhlmann N]] | ||
[[Category: Lammers | [[Category: Lammers M]] | ||
[[Category: Wroblowski | [[Category: Wroblowski S]] | ||
Revision as of 16:19, 26 July 2023
Double acetylated RhoGDI-alpha in complex with RhoA-GDPDouble acetylated RhoGDI-alpha in complex with RhoA-GDP
Structural highlights
FunctionGDIR1_BOVIN In glioma cells, inhibits cell migration and invasion by mediating the signals of SEMA5A and PLXNB3 that lead to inactivation of RAC1 (By similarity). Regulates the GDP/GTP exchange reaction of the Rho proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them.[1] [2] Publication Abstract from PubMedRho proteins are major regulators of the cytoskeleton. As most Ras-related proteins, they switch between an active, GTP-bound and an inactive, GDP-bound conformation. Rho proteins are targeted to the plasma membrane via a polybasic region and a prenyl group attached to a C-terminal cysteine residue. To distribute Rho proteins in the cell, the molecular chaperone RhoGDIalpha binds to the prenylated Rho proteins forming a cytosolic pool of mainly GDP-loaded Rho. Most studies characterized the interaction of prenylated Rho proteins and RhoGDIalpha. However, RhoGDIalpha was also shown to bind to nonprenylated Rho proteins with physiologically relevant micomolar affinities. Recently, it was discovered that RhoGDIalpha is targeted by post-translational lysine acetylation. For one site, K141, it was hypothesized that acetylation might lead to increased levels of formation of filamentous actin and filopodia in mammalian cells. The functional consequences of lysine acetylation for the interplay with nonprenylated RhoA have not been investigated. Here, we report that lysine acetylation at lysines K127 and K141 in the RhoGDIalpha immunoglobulin domain interferes with the interaction toward nonprenylated RhoA using a combined biochemical and biophysical approach. We determined the first crystal structure of a doubly acetylated protein, RhoGDIalpha, in complex with RhoA.GDP. We discover that the C-terminus of RhoA adopts a different conformation forming an intermolecular beta-sheet with the RhoGDIalpha immunoglobulin domain. RhoGDIalpha Acetylation at K127 and K141 Affects Binding toward Nonprenylated RhoA.,Kuhlmann N, Wroblowski S, Scislowski L, Lammers M Biochemistry. 2016 Jan 4. PMID:26695096[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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