5irc: Difference between revisions
New page: '''Unreleased structure''' The entry 5irc is ON HOLD Authors: Derewenda, U., Derewenda, Z. Description: p190A GAP domain complex with RhoA Category: Unreleased Structures [[Categor... |
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The | ==p190A GAP domain complex with RhoA== | ||
<StructureSection load='5irc' size='340' side='right'caption='[[5irc]], [[Resolution|resolution]] 1.72Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5irc]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IRC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IRC FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.72Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CSX:S-OXY+CYSTEINE'>CSX</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MGF:TRIFLUOROMAGNESATE'>MGF</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=5irc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5irc OCA], [https://pdbe.org/5irc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5irc RCSB], [https://www.ebi.ac.uk/pdbsum/5irc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5irc ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/RHG35_RAT RHG35_RAT] Represses transcription of the glucocorticoid receptor by binding to the cis-acting regulatory sequence 5'-GAGAAAAGAAACTGGAGAAACTC-3'. May transduce signals from p21-ras to the nucleus, acting via the ras GTPase-activating protein (GAP). May also act as a tumor suppressor (By similarity). | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Rho GTPase-activating proteins (RhoGAPs) are one of the major classes of regulators of the Rho-related protein family that are crucial in many cellular processes, motility, contractility, growth, differentiation, and development. Using database searches we extracted 66 distinct human RhoGAPs, from which 57 have got a common catalytic domain capable of terminating Rho protein signaling by stimulating the slow intrinsic GTP hydrolysis (GTPase) reaction. The specificity of the majority of the members of RhoGAP family is largely uncharacterized. Here, we comprehensively investigated the sequence-structure-function relationship between RhoGAPs and Rho proteins by combining our in vitro data with in silico data. The activity of 14 representatives of the RhoGAP family towards 12 Rho family proteins was determined in real-time. We identified and structurally verified hotspots in the interface between RhoGAPs and Rho proteins as critical determinants for binding and catalysis. We have found that the RhoGAP domain itself is nonselective and in some cases rather inefficient under cell-free conditions. Thus, we propose that other domains of RhoGAPs confer substrate specificity and fine-tune their catalytic efficiency in cells. | |||
Deciphering the molecular and functional basis of RhoGAP family proteins: A systematic approach towards selective inactivation of Rho family proteins.,Amin E, Jaiswal M, Derewenda U, Reis K, Nouri K, Koessmeier KT, Aspenstrom P, Somlyo AV, Dvorsky R, Ahmadian MR J Biol Chem. 2016 Aug 1. pii: jbc.M116.736967. PMID:27481945<ref>PMID:27481945</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Derewenda | <div class="pdbe-citations 5irc" style="background-color:#fffaf0;"></div> | ||
[[Category: Derewenda | |||
==See Also== | |||
*[[Rho GTPase 3D structures|Rho GTPase 3D structures]] | |||
*[[Rho GTPase activating protein 3D structures|Rho GTPase activating protein 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Rattus norvegicus]] | |||
[[Category: Derewenda U]] | |||
[[Category: Derewenda Z]] | |||
Latest revision as of 17:06, 30 August 2023
p190A GAP domain complex with RhoAp190A GAP domain complex with RhoA
Structural highlights
FunctionRHG35_RAT Represses transcription of the glucocorticoid receptor by binding to the cis-acting regulatory sequence 5'-GAGAAAAGAAACTGGAGAAACTC-3'. May transduce signals from p21-ras to the nucleus, acting via the ras GTPase-activating protein (GAP). May also act as a tumor suppressor (By similarity). Publication Abstract from PubMedRho GTPase-activating proteins (RhoGAPs) are one of the major classes of regulators of the Rho-related protein family that are crucial in many cellular processes, motility, contractility, growth, differentiation, and development. Using database searches we extracted 66 distinct human RhoGAPs, from which 57 have got a common catalytic domain capable of terminating Rho protein signaling by stimulating the slow intrinsic GTP hydrolysis (GTPase) reaction. The specificity of the majority of the members of RhoGAP family is largely uncharacterized. Here, we comprehensively investigated the sequence-structure-function relationship between RhoGAPs and Rho proteins by combining our in vitro data with in silico data. The activity of 14 representatives of the RhoGAP family towards 12 Rho family proteins was determined in real-time. We identified and structurally verified hotspots in the interface between RhoGAPs and Rho proteins as critical determinants for binding and catalysis. We have found that the RhoGAP domain itself is nonselective and in some cases rather inefficient under cell-free conditions. Thus, we propose that other domains of RhoGAPs confer substrate specificity and fine-tune their catalytic efficiency in cells. Deciphering the molecular and functional basis of RhoGAP family proteins: A systematic approach towards selective inactivation of Rho family proteins.,Amin E, Jaiswal M, Derewenda U, Reis K, Nouri K, Koessmeier KT, Aspenstrom P, Somlyo AV, Dvorsky R, Ahmadian MR J Biol Chem. 2016 Aug 1. pii: jbc.M116.736967. PMID:27481945[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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