4cdo: Difference between revisions
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<StructureSection load='4cdo' size='340' side='right' caption='[[4cdo]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='4cdo' size='340' side='right' caption='[[4cdo]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4cdo]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CDO OCA]. <br> | <table><tr><td colspan='2'>[[4cdo]] is a 2 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=4CDO OCA]. <br> | ||
</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> | </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>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4cdo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cdo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cdo RCSB], [http://www.ebi.ac.uk/pdbsum/4cdo PDBsum]</span></td></tr> | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4cdo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cdo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cdo RCSB], [http://www.ebi.ac.uk/pdbsum/4cdo PDBsum]</span></td></tr> | ||
<table> | <table> | ||
<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. | |||
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> | |||
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.]] | ||