4nwy
From Proteopedia
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| - | + | ==Crystal structure of the b' domain of human protein disulfide isomerase-like protein of the testis (PDILT)== | |
| - | + | <StructureSection load='4nwy' size='340' side='right' caption='[[4nwy]], [[Resolution|resolution]] 2.00Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4nwy]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NWY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NWY FirstGlance]. <br> | |
| - | ==Function== | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene></td></tr> |
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PDILT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4nwy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nwy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nwy RCSB], [http://www.ebi.ac.uk/pdbsum/4nwy PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
[[http://www.uniprot.org/uniprot/PDILT_HUMAN PDILT_HUMAN]] Probable redox-inactive chaperone involved in spermatogenesis.<ref>PMID:17507649</ref> | [[http://www.uniprot.org/uniprot/PDILT_HUMAN PDILT_HUMAN]] Probable redox-inactive chaperone involved in spermatogenesis.<ref>PMID:17507649</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Protein Disulfide Isomerase-Like protein of the Testis (PDILT) is a testis-specific member of the PDI family. PDILT displays similar domain architecture to PDIA1, the founding member of this protein family, but lacks catalytic cysteines needed for oxidoreduction reactions. This suggests special importance of chaperone activity of PDILT, but how it recognizes misfolded protein substrates is unknown. Here, we report the high-resolution crystal structure of the b' domain of human PDILT. The structure reveals a conserved hydrophobic pocket, which is likely a principal substrate-binding site in PDILT. In the crystal, this pocket is occupied by side chains of tyrosine and tryptophan residues from another PDILT molecule, suggesting a preference for binding exposed aromatic residues in protein substrates. The lack of interaction of the b' domain with the P-domains of calreticulin-3 and calmegin hints at a novel way of interaction between testis-specific lectin chaperones and PDILT. Further studies of this recently discovered PDI member would help to understand the important role that PDILT plays in the differentiation and maturation of spermatozoids. | ||
| - | + | Structure of the substrate-binding b' domain of the Protein disulfide isomerase-like protein of the testis.,Bastos-Aristizabal S, Kozlov G, Gehring K Sci Rep. 2014 Mar 25;4:4464. doi: 10.1038/srep04464. PMID:24662985<ref>PMID:24662985</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Human]] | ||
[[Category: Protein disulfide-isomerase]] | [[Category: Protein disulfide-isomerase]] | ||
| - | [[Category: Bastos-Aristizabal, S | + | [[Category: Bastos-Aristizabal, S]] |
| - | [[Category: Gehring, K | + | [[Category: Gehring, K]] |
| - | [[Category: Kozlov, G | + | [[Category: Kozlov, G]] |
[[Category: Endoplasmic reticulum]] | [[Category: Endoplasmic reticulum]] | ||
[[Category: Isomerase]] | [[Category: Isomerase]] | ||
[[Category: Substrate-binding domain]] | [[Category: Substrate-binding domain]] | ||
[[Category: Thioredoxin-like fold]] | [[Category: Thioredoxin-like fold]] | ||
Revision as of 18:34, 25 December 2014
Crystal structure of the b' domain of human protein disulfide isomerase-like protein of the testis (PDILT)
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