1mek

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[[Image:1mek.png|left|200px]]
 
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==HUMAN PROTEIN DISULFIDE ISOMERASE, NMR, 40 STRUCTURES==
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The line below this paragraph, containing "STRUCTURE_1mek", creates the "Structure Box" on the page.
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<StructureSection load='1mek' size='340' side='right'caption='[[1mek]]' 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'>[[1mek]] 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=1MEK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MEK 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, 40 models</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=1mek FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mek OCA], [https://pdbe.org/1mek PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mek RCSB], [https://www.ebi.ac.uk/pdbsum/1mek PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mek ProSAT]</span></td></tr>
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{{STRUCTURE_1mek| PDB=1mek | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PDIA1_HUMAN PDIA1_HUMAN] This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP.<ref>PMID:10636893</ref> <ref>PMID:12485997</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/me/1mek_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=1mek 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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As a first step in dissecting the structure of human protein disulfide isomerase (PDI), the structure of a fragment corresponding to the first 120 residues of its sequence has been determined using heteronuclear multidimensional NMR techniques. As expected from its primary structure homology, the fragment has the thioredoxin fold. Similarities and differences in their structures help to explain why thioredoxins are reductants, whereas PDI is an oxidant of protein thiol groups. The results confirm that PDI has a modular, multidomain structure, which will facilitate its structural and functional characterization.
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===HUMAN PROTEIN DISULFIDE ISOMERASE, NMR, 40 STRUCTURES===
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Structure determination of the N-terminal thioredoxin-like domain of protein disulfide isomerase using multidimensional heteronuclear 13C/15N NMR spectroscopy.,Kemmink J, Darby NJ, Dijkstra K, Nilges M, Creighton TE Biochemistry. 1996 Jun 18;35(24):7684-91. PMID:8672469<ref>PMID:8672469</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_8672469}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1mek" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 8672469 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_8672469}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1MEK is a 1 chain structure of sequence 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=1MEK OCA].
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==Reference==
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<ref group="xtra">PMID:8672469</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Protein disulfide-isomerase]]
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[[Category: Large Structures]]
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[[Category: Creighton, T E.]]
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[[Category: Creighton TE]]
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[[Category: Darby, N J.]]
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[[Category: Darby NJ]]
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[[Category: Dijkstra, K.]]
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[[Category: Dijkstra K]]
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[[Category: Kemmink, J.]]
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[[Category: Kemmink J]]
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[[Category: Nilges, M.]]
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[[Category: Nilges M]]
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[[Category: Electron transport]]
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[[Category: Endoplasmic reticulum]]
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[[Category: Isomerase]]
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[[Category: Redox-active center]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 02:44:23 2009''
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HUMAN PROTEIN DISULFIDE ISOMERASE, NMR, 40 STRUCTURES

PDB ID 1mek

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