1htj

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[[Image:1htj.jpg|left|200px]]<br /><applet load="1htj" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1htj, resolution 2.2&Aring;" />
 
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'''STRUCTURE OF THE RGS-LIKE DOMAIN FROM PDZ-RHOGEF'''<br />
 
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==Overview==
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==STRUCTURE OF THE RGS-LIKE DOMAIN FROM PDZ-RHOGEF==
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BACKGROUND: The multidomain PDZ-RhoGEF is one of many known guanine nucleotide exchange factors that upregulate Rho GTPases. PDZ-RhoGEF and related family members play a critical role in a molecular signaling pathway from heterotrimeric G protein-coupled receptors to Rho proteins. A approximately 200 residue RGS-like (RGSL) domain in PDZ-RhoGEF and its homologs is responsible for the direct association with Galpha12/13 proteins. To better understand structure-function relationships, we initiated crystallographic studies of the RGSL domain from human PDZ-RhoGEF. RESULTS: A recombinant construct of the RGSL domain was expressed in Escherichia coli and purified, but it did not crystallize. Alternative constructs were designed based on a novel strategy of targeting lysine and glutamic acid residues for mutagenesis to alanine. A triple-point mutant functionally identical to the wild-type protein was crystallized, and its structure was determined by the MAD method using Se-methionine (Se-Met) incorporation. A molecular model of the RGSL domain was refined at 2.2 A resolution, revealing an all-helical tertiary fold with the mutations located at intermolecular lattice contacts. CONCLUSIONS: The first nine helices adopt a fold similar to that observed for RGS proteins, although the sequence identity with other such known structures is below 20%. The last three helices are an integral extension of the RGS fold, packing tightly against helices 3 and 4 with multiple hydrophobic interactions. Comparison with RGS proteins suggests features that are likely relevant for interaction with G proteins. Finally, we conclude that the strategy used to produce crystals was beneficial and might be applicable to other proteins resistant to crystallization.
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<StructureSection load='1htj' size='340' side='right'caption='[[1htj]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1htj]] is a 1 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=1HTJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HTJ FirstGlance]. <br>
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1HTJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HTJ OCA].
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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]] 2.2&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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==Reference==
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1htj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1htj OCA], [https://pdbe.org/1htj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1htj RCSB], [https://www.ebi.ac.uk/pdbsum/1htj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1htj ProSAT]</span></td></tr>
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Structure of the RGS-like domain from PDZ-RhoGEF: linking heterotrimeric g protein-coupled signaling to Rho GTPases., Longenecker KL, Lewis ME, Chikumi H, Gutkind JS, Derewenda ZS, Structure. 2001 Jul 3;9(7):559-69. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11470431 11470431]
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ARHGB_HUMAN ARHGB_HUMAN] May play a role in the regulation of RhoA GTPase by guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13). Acts as guanine nucleotide exchange factor (GEF) for RhoA GTPase and may act as GTPase-activating protein (GAP) for GNA12 and GNA13.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ht/1htj_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1htj ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Chikumi, H.]]
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[[Category: Chikumi H]]
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[[Category: Derewenda, Z S.]]
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[[Category: Derewenda ZS]]
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[[Category: Gutkind, J S.]]
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[[Category: Gutkind JS]]
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[[Category: Lewis, M E.]]
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[[Category: Lewis ME]]
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[[Category: Longenecker, K L.]]
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[[Category: Longenecker KL]]
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[[Category: gef]]
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[[Category: guanine nucleotide exchange factor]]
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[[Category: regulator of g protein signaling]]
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[[Category: rgs-like]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:04:47 2008''
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Current revision

STRUCTURE OF THE RGS-LIKE DOMAIN FROM PDZ-RHOGEF

PDB ID 1htj

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