3hpm

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[[Image:3hpm.png|left|200px]]
 
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==Oxidized dimeric PICK1 PDZ C46G mutant in complex with the carboxyl tail peptide of GluR2==
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The line below this paragraph, containing "STRUCTURE_3hpm", creates the "Structure Box" on the page.
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<StructureSection load='3hpm' size='340' side='right'caption='[[3hpm]], [[Resolution|resolution]] 2.80&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'>[[3hpm]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HPM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HPM 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">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</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=3hpm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hpm OCA], [https://pdbe.org/3hpm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hpm RCSB], [https://www.ebi.ac.uk/pdbsum/3hpm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hpm ProSAT]</span></td></tr>
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{{STRUCTURE_3hpm| PDB=3hpm | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PICK1_RAT PICK1_RAT] Probable adapter protein that bind to and organize the subcellular localization of a variety of membrane proteins containing some PDZ recognition sequence. Involved in the clustering of various receptors, possibly by acting at the receptor internalization level. Plays a role in synaptic plasticity by regulating the trafficking and internalization of AMPA receptors. May be regulated upon PRKCA activation. May regulate ASIC1/ASIC3 channel.<ref>PMID:16138078</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/hp/3hpm_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=3hpm 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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PICK1 is a PDZ/BAR domain-containing scaffold protein that regulates the trafficking of many receptors and ion channels, including AMPA receptors. In addition to binding to a wide spectrum of target proteins to be transported, the PICK1 PDZ domain, via its conserved CPC motif, has also been shown to bind to lipid membranes. However, the molecular basis of the CPC motif-mediated lipid membrane binding of the PICK1 PDZ domain is not known. Here we show that the Cys residues in the CPC motif of the PICK1 PDZ domain forms reversible, intermolecular disulfide bonds under mild oxidation conditions. Importantly, formation of the disulfide-mediated dimer abolishes the lipid membrane binding capacity of the PICK1 PDZ domain and thereby is expected to alter the cellular functions of PICK1. The structures of the PDZ dimers provide atomic-scale pictures of disulfide-mediated PICK1 dimer formation and a molecular explanation of the oxidation-induced dissociation of PICK1 from membranes. We propose that the PICK1-mediated trafficking processes might be regulated by cellular redox fluctuations under both physiological and pathophysiological conditions.
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===Oxidized dimeric PICK1 PDZ C46G mutant in complex with the carboxyl tail peptide of GluR2===
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Redox-regulated lipid membrane binding of the PICK1 PDZ domain.,Shi Y, Yu J, Jia Y, Pan L, Shen C, Xia J, Zhang M Biochemistry. 2010 Jun 1;49(21):4432-9. PMID:20426484<ref>PMID:20426484</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_20426484}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 3hpm" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 20426484 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_20426484}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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[[3hpm]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus,_synthetic Rattus norvegicus, synthetic]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HPM OCA].
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[[Category: Rattus norvegicus]]
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[[Category: Synthetic construct]]
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==Reference==
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[[Category: Shi Y]]
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<ref group="xtra">PMID:20426484</ref><references group="xtra"/>
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[[Category: Yu J]]
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[[Category: Rattus norvegicus, synthetic]]
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[[Category: Zhang M]]
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[[Category: Shi, Y.]]
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[[Category: Yu, J.]]
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[[Category: Zhang, M.]]
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[[Category: Oxidized]]
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[[Category: Pdz domain]]
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[[Category: Protein binding]]
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Current revision

Oxidized dimeric PICK1 PDZ C46G mutant in complex with the carboxyl tail peptide of GluR2

PDB ID 3hpm

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