2oqs

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{{Seed}}
 
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[[Image:2oqs.png|left|200px]]
 
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==Structure of the hDLG/SAP97 PDZ2 in complex with HPV-18 papillomavirus E6 peptide==
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The line below this paragraph, containing "STRUCTURE_2oqs", creates the "Structure Box" on the page.
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<StructureSection load='2oqs' size='340' side='right'caption='[[2oqs]]' 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'>[[2oqs]] is a 2 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=2OQS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OQS FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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=2oqs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oqs OCA], [https://pdbe.org/2oqs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2oqs RCSB], [https://www.ebi.ac.uk/pdbsum/2oqs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2oqs ProSAT]</span></td></tr>
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{{STRUCTURE_2oqs| PDB=2oqs | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/DLG1_HUMAN DLG1_HUMAN] Essential multidomain scaffolding protein required for normal development (By similarity). Recruits channels, receptors and signaling molecules to discrete plasma membrane domains in polarized cells. May play a role in adherens junction assembly, signal transduction, cell proliferation, synaptogenesis and lymphocyte activation. Regulates the excitability of cardiac myocytes by modulating the functional expression of Kv4 channels. Functional regulator of Kv1.5 channel.<ref>PMID:10656683</ref> <ref>PMID:12445884</ref> <ref>PMID:14699157</ref> <ref>PMID:15263016</ref> <ref>PMID:19213956</ref> <ref>PMID:20605917</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/oq/2oqs_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=2oqs 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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The E6 protein from high-risk types of human papillomavirus (HPV) binds PDZ-domain containing proteins and targets them for degradation. We used isothermal titration calorimetry to measure the interaction of a peptide from the C-terminus of HPV-18 E6 to the second PDZ domain (PDZ2) from the human homologue of the Drosophila discs large tumor suppressor protein (hDlg). Isothermal titration calorimetry experiments with a series of peptides showed that HPV-18 E6 bound hDlg PDZ2 about 5-fold stronger than HPV-16 E6, that the contribution of Arg154 to binding was about 1 kcal/mol, and that the binding was disabled by phosphorylation at Thr156. We then used NMR to determine the solution structure of the complex of PDZ2 bound to the HPV-18 E6 peptide. The resultant structures were of high quality and had backbone root-mean-square deviations of less than 0.5 A. The structure shows a novel mode of interaction in which six residues of the HPV-18 E6 peptide are contacted by the PDZ2 domain, in contrast to the typical four residues used by class I PDZ domains. Molecular dynamics simulations supported a model in which the C- and N-terminal ends of the peptide had different mobilities within the complex. Comparison of the NMR complex structure to previously determined X-ray structures of PDZ2 by itself and bound to different peptides allows a description of conformational changes required for PDZ2 to bind to HPV-18 E6.
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===Structure of the hDLG/SAP97 PDZ2 in complex with HPV-18 papillomavirus E6 peptide===
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Solution structure of the hDlg/SAP97 PDZ2 domain and its mechanism of interaction with HPV-18 papillomavirus E6 protein.,Liu Y, Henry GD, Hegde RS, Baleja JD Biochemistry. 2007 Sep 25;46(38):10864-74. Epub 2007 Aug 22. PMID:17713926<ref>PMID:17713926</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_17713926}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2oqs" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 17713926 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_17713926}}
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__TOC__
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</StructureSection>
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==About this Structure==
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2OQS is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OQS OCA].
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==Reference==
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<ref group="xtra">PMID:17713926</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Baleja, J D.]]
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[[Category: Large Structures]]
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[[Category: Hegde, R S.]]
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[[Category: Baleja JD]]
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[[Category: Henry, G D.]]
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[[Category: Hegde RS]]
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[[Category: Liu, Y.]]
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[[Category: Henry GD]]
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[[Category: Hdlg pdz domain]]
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[[Category: Liu Y]]
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[[Category: Hpv e6]]
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[[Category: Peptide-binding protein]]
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[[Category: Protein-peptide complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 09:21:06 2009''
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Current revision

Structure of the hDLG/SAP97 PDZ2 in complex with HPV-18 papillomavirus E6 peptide

PDB ID 2oqs

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