1kjy

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[[Image:1kjy.png|left|200px]]
 
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==Crystal Structure of Human G[alpha]i1 Bound to the GoLoco Motif of RGS14==
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The line below this paragraph, containing "STRUCTURE_1kjy", creates the "Structure Box" on the page.
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<StructureSection load='1kjy' size='340' side='right'caption='[[1kjy]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1kjy]] 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=1KJY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KJY FirstGlance]. <br>
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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]] 2.7&#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=CS:CESIUM+ION'>CS</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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{{STRUCTURE_1kjy| PDB=1kjy | SCENE= }}
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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=1kjy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kjy OCA], [https://pdbe.org/1kjy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kjy RCSB], [https://www.ebi.ac.uk/pdbsum/1kjy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kjy ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GNAI1_HUMAN GNAI1_HUMAN] Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. The G(i) proteins are involved in hormonal regulation of adenylate cyclase: they inhibit the cyclase in response to beta-adrenergic stimuli. The inactive GDP-bound form prevents the association of RGS14 with centrosomes and is required for the translocation of RGS14 from the cytoplasm to the plasma membrane. May play a role in cell division.<ref>PMID:17635935</ref> <ref>PMID:17264214</ref>
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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/kj/1kjy_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=1kjy ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Heterotrimeric G-proteins bind to cell-surface receptors and are integral in transmission of signals from outside the cell. Upon activation of the Galpha subunit by binding of GTP, the Galpha and Gbetagamma subunits dissociate and interact with effector proteins for signal transduction. Regulatory proteins with the 19-amino-acid GoLoco motif can bind to Galpha subunits and maintain G-protein subunit dissociation in the absence of Galpha activation. Here we describe the structural determinants of GoLoco activity as revealed by the crystal structure of Galpha(i1) GDP bound to the GoLoco region of the 'regulator of G-protein signalling' protein RGS14. Key contacts are described between the GoLoco motif and Galpha protein, including the extension of GoLoco's highly conserved Asp/Glu-Gln-Arg triad into the nucleotide-binding pocket of Galpha to make direct contact with the GDP alpha- and beta-phosphates. The structural organization of the GoLoco Galpha(i1) complex, when combined with supporting data from domain-swapping experiments, suggests that the Galpha all-helical domain and GoLoco-region carboxy-terminal residues control the specificity of GoLoco Galpha interactions.
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===Crystal Structure of Human G[alpha]i1 Bound to the GoLoco Motif of RGS14===
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Structural determinants for GoLoco-induced inhibition of nucleotide release by Galpha subunits.,Kimple RJ, Kimple ME, Betts L, Sondek J, Siderovski DP Nature. 2002 Apr 25;416(6883):878-81. PMID:11976690<ref>PMID:11976690</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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The line below this paragraph, {{ABSTRACT_PUBMED_11976690}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1kjy" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 11976690 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_11976690}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[1kjy]] is a 4 chain structure with 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=1KJY OCA].
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==Reference==
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<ref group="xtra">PMID:011976690</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Betts, L.]]
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[[Category: Large Structures]]
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[[Category: Kimple, M E.]]
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[[Category: Rattus norvegicus]]
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[[Category: Kimple, R J.]]
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[[Category: Betts L]]
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[[Category: Siderovski, D P.]]
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[[Category: Kimple ME]]
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[[Category: Sondek, J.]]
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[[Category: Kimple RJ]]
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[[Category: Protein-peptide complex]]
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[[Category: Siderovski DP]]
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[[Category: Signaling protein]]
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[[Category: Sondek J]]

Current revision

Crystal Structure of Human G[alpha]i1 Bound to the GoLoco Motif of RGS14

PDB ID 1kjy

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