2k85

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{{Seed}}
 
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[[Image:2k85.jpg|left|200px]]
 
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==p190-A RhoGAP FF1 domain==
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The line below this paragraph, containing "STRUCTURE_2k85", creates the "Structure Box" on the page.
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<StructureSection load='2k85' size='340' side='right'caption='[[2k85]]' 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'>[[2k85]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K85 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2K85 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">Solution NMR</td></tr>
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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=2k85 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k85 OCA], [https://pdbe.org/2k85 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2k85 RCSB], [https://www.ebi.ac.uk/pdbsum/2k85 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2k85 ProSAT]</span></td></tr>
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{{STRUCTURE_2k85| PDB=2k85 | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/RHG35_HUMAN RHG35_HUMAN] Represses transcription of the glucocorticoid receptor by binding to the cis-acting regulatory sequence 5'-GAGAAAAGAAACTGGAGAAACTC-3'. May participate in the regulation of retinal development and degeneration. May transduce signals from p21-ras to the nucleus, acting via the ras GTPase-activating protein (GAP). May also act as a tumor suppressor.<ref>PMID:1894621</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/k8/2k85_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=2k85 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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p190-A and -B Rho GAPs (guanosine triphosphatase activating proteins) are the only cytoplasmatic proteins containing FF domains. In p190-A Rho GAP, the region containing the FF domains has been implicated in binding to the transcription factor TFII-I. Moreover, phosphorylation of Tyr308 within the first FF domain inhibits this interaction. Because the structural determinants governing this mechanism remain unknown, we sought to solve the structure of the first FF domain of p190-A Rho GAP (RhoGAPFF1) and to study the potential impact of phosphorylation on the structure. We found that RhoGAPFF1 does not fold with the typical (alpha1-alpha2-3(10)-alpha 3) arrangement of other FF domains. Instead, the NMR data obtained at 285 K show an alpha1-alpha2-alpha 3-alpha 4 topology. In addition, we observed that specific contacts between residues in the first loop and the fourth helix are indispensable for the correct folding and stability of this domain. The structure also revealed that Tyr308 contributes to the domain hydrophobic core. Furthermore, the residues that compose the target motif of the platelet-derived growth factor receptor alpha kinase form part of the alpha 3 helix. We observed that the phosphorylation reaction requires a previous step including domain unfolding, a process that occurs at 310 K. In the absence of phosphorylation, the temperature-dependent RhoGAPFF1 folding/unfolding process is reversible. However, phosphorylation causes an irreversible destabilization of the RhoGAPFF1 structure, which probably accounts for the inhibitory effect that it exerts on the TFII-I interaction. Our results link the ability of a protein domain to be phosphorylated with conformational changes in its three-dimensional structure.
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===p190-A RhoGAP FF1 domain===
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NMR structural studies on human p190-A RhoGAPFF1 revealed that domain phosphorylation by the PDGF-receptor alpha requires its previous unfolding.,Bonet R, Ruiz L, Aragon E, Martin-Malpartida P, Macias MJ J Mol Biol. 2009 Jun 5;389(2):230-7. Epub 2009 Apr 22. PMID:19393245<ref>PMID:19393245</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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The line below this paragraph, {{ABSTRACT_PUBMED_19393245}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2k85" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 19393245 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_19393245}}
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__TOC__
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</StructureSection>
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==About this Structure==
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2K85 is a 1 chain 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=2K85 OCA].
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==Reference==
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<ref group="xtra">PMID:19393245</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Bonet, R.]]
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[[Category: Large Structures]]
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[[Category: Macias, M.]]
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[[Category: Bonet R]]
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[[Category: Martin-Malpartida, P.]]
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[[Category: Macias M]]
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[[Category: Ruiz, L.]]
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[[Category: Martin-Malpartida P]]
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[[Category: Alternative splicing]]
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[[Category: Ruiz L]]
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[[Category: Anti-oncogene]]
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[[Category: Cell cycle]]
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[[Category: Cytoplasm]]
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[[Category: Dna-binding]]
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[[Category: Ff domain]]
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[[Category: Gtpase activation]]
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[[Category: Nucleus]]
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[[Category: P190-a rhogap]]
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[[Category: Phosphoprotein]]
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[[Category: Protein binding]]
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[[Category: Protein phosphorylation]]
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[[Category: Repressor]]
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[[Category: Transcription]]
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[[Category: Transcription regulation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 20 17:00:49 2009''
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Current revision

p190-A RhoGAP FF1 domain

PDB ID 2k85

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