4cdo: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Crystal structure of PQBP1 bound to spliceosomal U5-15kD== | ==Crystal structure of PQBP1 bound to spliceosomal U5-15kD== | ||
<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 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CDO FirstGlance]. <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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CDO FirstGlance]. <br> | ||
</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=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> | </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=4cdo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cdo OCA], [http://pdbe.org/4cdo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4cdo RCSB], [http://www.ebi.ac.uk/pdbsum/4cdo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4cdo ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| Line 15: | Line 16: | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4cdo" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 00:06, 5 August 2016
Crystal structure of PQBP1 bound to spliceosomal U5-15kDCrystal structure of PQBP1 bound to spliceosomal U5-15kD
Structural highlights
Function[TXN4A_HUMAN] Essential role in pre-mRNA splicing. Publication Abstract from PubMedA 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||