4cek: Difference between revisions
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==Crystal structure of the second MIF4G domain of human nonsense mediated decay factor UPF2== | |||
<StructureSection load='4cek' size='340' side='right' caption='[[4cek]], [[Resolution|resolution]] 2.35Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4cek]] is a 1 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=4CEK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CEK FirstGlance]. <br> | |||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cem|4cem]]</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=4cek FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cek OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cek RCSB], [http://www.ebi.ac.uk/pdbsum/4cek PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Nonsense-mediated decay (NMD) is a eukaryotic quality control pathway, involving conserved proteins UPF1, UPF2 and UPF3b, which detects and degrades mRNAs with premature stop codons. Human UPF2 comprises three tandem MIF4G domains and a C-terminal UPF1 binding region. MIF4G-3 binds UPF3b, but the specific functions of MIF4G-1 and MIF4G-2 are unknown. Crystal structures show that both MIF4G-1 and MIF4G-2 contain N-terminal capping helices essential for stabilization of the 10-helix MIF4G core and that MIF4G-2 interacts with MIF4G-3, forming a rigid assembly. The UPF2/UPF3b/SMG1 complex is thought to activate the kinase SMG1 to phosphorylate UPF1 in vivo. We identify MIF4G-3 as the binding site and in vitro substrate of SMG1 kinase and show that a ternary UPF2 MIF4G-3/UPF3b/SMG1 complex can form in vitro. Whereas in vivo complementation assays show that MIF4G-1 and MIF4G-2 are essential for NMD, tethering assays reveal that UPF2 truncated to only MIF4G-3 and the UPF1-binding region can still partially accomplish NMD. Thus UPF2 MIF4G-1 and MIF4G-2 appear to have a crucial scaffolding role, while MIF4G-3 is the key module required for triggering NMD. | |||
Structural and functional analysis of the three MIF4G domains of nonsense-mediated decay factor UPF2.,Clerici M, Deniaud A, Boehm V, Gehring NH, Schaffitzel C, Cusack S Nucleic Acids Res. 2013 Nov 23. PMID:24271394<ref>PMID:24271394</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
== | <references/> | ||
__TOC__ | |||
[[Category: Boehm, V | </StructureSection> | ||
[[Category: Clerici, M | [[Category: Human]] | ||
[[Category: Cusack, S | [[Category: Boehm, V]] | ||
[[Category: Deniaud, A | [[Category: Clerici, M]] | ||
[[Category: Gehring, N H | [[Category: Cusack, S]] | ||
[[Category: Schaffitzel, C | [[Category: Deniaud, A]] | ||
[[Category: Gehring, N H]] | |||
[[Category: Schaffitzel, C]] | |||
[[Category: Transcription]] | [[Category: Transcription]] | ||
Revision as of 16:34, 21 December 2014
Crystal structure of the second MIF4G domain of human nonsense mediated decay factor UPF2
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