4bws
From Proteopedia
(Difference between revisions)
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<StructureSection load='4bws' size='340' side='right' caption='[[4bws]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='4bws' size='340' side='right' caption='[[4bws]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[4bws]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BWS OCA]. <br> | + | <table><tr><td colspan='2'>[[4bws]] is a 6 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=4BWS OCA]. <br> |
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4bwq|4bwq]]</td></tr> | </td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4bwq|4bwq]]</td></tr> | ||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr> | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr> | ||
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/TXN4A_HUMAN TXN4A_HUMAN]] Essential role in pre-mRNA splicing. [[http://www.uniprot.org/uniprot/PQBP1_HUMAN PQBP1_HUMAN]] May suppress the ability of POU3F2 to transactivate the DRD1 gene in a POU3F2 dependent manner. Can activate transcription directly or via association with the transcription machinery. May be involved in ATXN1 mutant-induced cell death. The interaction with ATXN1 mutant reduces levels of phosphorylated RNA polymerase II large subunit.<ref>PMID:10332029</ref> <ref>PMID:10198427</ref> <ref>PMID:12062018</ref> | [[http://www.uniprot.org/uniprot/TXN4A_HUMAN TXN4A_HUMAN]] Essential role in pre-mRNA splicing. [[http://www.uniprot.org/uniprot/PQBP1_HUMAN PQBP1_HUMAN]] May suppress the ability of POU3F2 to transactivate the DRD1 gene in a POU3F2 dependent manner. Can activate transcription directly or via association with the transcription machinery. May be involved in ATXN1 mutant-induced cell death. The interaction with ATXN1 mutant reduces levels of phosphorylated RNA polymerase II large subunit.<ref>PMID:10332029</ref> <ref>PMID:10198427</ref> <ref>PMID:12062018</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | A loss-of-function of polyglutamine tract-binding protein 1 (PQBP1) induced by frameshift mutations is believed to cause X-linked mental retardation. However, the mechanism by which structural changes in PQBP1 lead to mental retardation is unknown. Here we present the crystal structure of a C-terminal fragment of PQBP1 in complex with the spliceosomal protein U5-15kD. The U5-15kD hydrophobic groove recognizes a YxxPxxVL motif in PQBP1, and mutations within this motif cause a loss-of-function phenotype of PQBP1 in vitro. The YxxPxxVL motif is absent in all PQBP1 frameshift mutants seen in cases of mental retardation. These results suggest a mechanism by which the loss of the YxxPxxVL motif could lead to the functional defects seen in this type of mental retardation. | ||
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| + | Mutations in the PQBP1 gene prevent its interaction with the spliceosomal protein U5-15kD.,Mizuguchi M, Obita T, Serita T, Kojima R, Nabeshima Y, Okazawa H Nat Commun. 2014 Apr 30;5:3822. doi: 10.1038/ncomms4822. PMID:24781215<ref>PMID:24781215</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Human]] | ||
[[Category: Kojima, R.]] | [[Category: Kojima, R.]] | ||
[[Category: Mizuguchi, M.]] | [[Category: Mizuguchi, M.]] | ||
Revision as of 06:57, 14 May 2014
Crystal structure of the heterotrimer of PQBP1, U5-15kD and U5-52kD.
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