8gdy
From Proteopedia
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- | '''Unreleased structure''' | ||
- | + | ==Crystal structure of the human PDI first domain with 9 mutations== | |
- | + | <StructureSection load='8gdy' size='340' side='right'caption='[[8gdy]], [[Resolution|resolution]] 2.05Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[8gdy]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8GDY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8GDY FirstGlance]. <br> | |
- | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.05Å</td></tr> | |
- | [[Category: | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SCN:THIOCYANATE+ION'>SCN</scene></td></tr> |
- | [[Category: | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8gdy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8gdy OCA], [https://pdbe.org/8gdy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8gdy RCSB], [https://www.ebi.ac.uk/pdbsum/8gdy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8gdy ProSAT]</span></td></tr> |
- | [[Category: Forouhar | + | </table> |
- | [[Category: | + | == Function == |
- | [[Category: | + | [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> |
- | [[Category: Hunt | + | == References == |
- | [[Category: | + | <references/> |
- | [[Category: | + | __TOC__ |
- | [[Category: | + | </StructureSection> |
- | [[Category: | + | [[Category: Homo sapiens]] |
+ | [[Category: Large Structures]] | ||
+ | [[Category: Banayan NE]] | ||
+ | [[Category: Forouhar F]] | ||
+ | [[Category: Handelman SK]] | ||
+ | [[Category: Hunt HS]] | ||
+ | [[Category: Hunt JF]] | ||
+ | [[Category: Loughlin BL]] | ||
+ | [[Category: Price N]] | ||
+ | [[Category: Singh S]] | ||
+ | [[Category: Wong V]] |
Current revision
Crystal structure of the human PDI first domain with 9 mutations
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Categories: Homo sapiens | Large Structures | Banayan NE | Forouhar F | Handelman SK | Hunt HS | Hunt JF | Loughlin BL | Price N | Singh S | Wong V