4i6x
From Proteopedia
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| - | + | ==Crystal Structure of Non-catalyic Domain of Protein Disulfide Isomerase-related (PDIr) Protein== | |
| - | + | <StructureSection load='4i6x' size='340' side='right' caption='[[4i6x]], [[Resolution|resolution]] 1.50Å' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[4i6x]] is a 1 chain structure with 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=4I6X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4I6X FirstGlance]. <br> | ||
| + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PDIA5, PDIR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein_disulfide-isomerase Protein disulfide-isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.4.1 5.3.4.1] </span></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4i6x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i6x OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4i6x RCSB], [http://www.ebi.ac.uk/pdbsum/4i6x PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Protein disulfide isomerases comprise a large family of enzymes responsible for catalyzing the proper oxidation and folding of newly synthesized proteins in the endoplasmic reticulum (ER). Protein disulfide isomerase-related (PDIR) protein (also known as PDIA5) is a specialized member that participates in the folding of alpha1-antitrypsin and N-linked glycoproteins. Here, the crystal structure of the non-catalytic domain of PDIR was determined to 1.5 A resolution. The structure adopts a thioredoxin-like fold stabilized by a structural disulfide bridge with a positively charged binding surface for interactions with the ER chaperones, calreticulin and ERp72. Crystal contacts between molecules potentially mimic the interactions of PDIR with misfolded substrate proteins. The results suggest that the non-catalytic domain of PDIR plays a key role in the recognition of protein partners and substrates. | ||
| - | + | Structure of the Non-Catalytic Domain of the Protein Disulfide Isomerase-Related Protein (PDIR) Reveals Function in Protein Binding.,Vinaik R, Kozlov G, Gehring K PLoS One. 2013 Apr 16;8(4):e62021. doi: 10.1371/journal.pone.0062021. Print 2013. PMID:23614004<ref>PMID:23614004</ref> | |
| - | + | ||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein disulfide-isomerase]] | [[Category: Protein disulfide-isomerase]] | ||
| - | [[Category: Gehring, K | + | [[Category: Gehring, K]] |
| - | [[Category: Kozlov, G | + | [[Category: Kozlov, G]] |
| - | [[Category: Vinaik, R | + | [[Category: Vinaik, R]] |
[[Category: Endoplasmic reticulum]] | [[Category: Endoplasmic reticulum]] | ||
[[Category: Isomerase]] | [[Category: Isomerase]] | ||
[[Category: Protein binding]] | [[Category: Protein binding]] | ||
[[Category: Thioredoxin-like fold]] | [[Category: Thioredoxin-like fold]] | ||
Revision as of 12:48, 4 January 2015
Crystal Structure of Non-catalyic Domain of Protein Disulfide Isomerase-related (PDIr) Protein
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