1hl6: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==A | |||
==A novel mode of RBD-protein recognition in the Y14-mago complex== | |||
<StructureSection load='1hl6' size='340' side='right' caption='[[1hl6]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='1hl6' size='340' side='right' caption='[[1hl6]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1hl6]] is a 4 chain structure | <table><tr><td colspan='2'>[[1hl6]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HL6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HL6 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=1hl6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hl6 OCA], [http://pdbe.org/1hl6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hl6 RCSB], [http://www.ebi.ac.uk/pdbsum/1hl6 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=1hl6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hl6 OCA], [http://pdbe.org/1hl6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hl6 RCSB], [http://www.ebi.ac.uk/pdbsum/1hl6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1hl6 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| Line 15: | Line 16: | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1hl6 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
| Line 30: | Line 31: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Conti, E]] | [[Category: Conti, E]] | ||
[[Category: Fribourg, S]] | [[Category: Fribourg, S]] | ||
Revision as of 07:28, 21 September 2017
A novel mode of RBD-protein recognition in the Y14-mago complexA novel mode of RBD-protein recognition in the Y14-mago complex
Structural highlights
Function[RBM8A_DROME] Involved in mRNA quality control via the nonsense-mediated mRNA decay (NMD) pathway. Also involved in localization of osk (oskar) mRNA in the posterior pole of oocytes via its interaction with mago.[1] [2] [MGN_DROME] Participates in the bidirectional intercellular signaling between the posterior follicle cells and oocyte to establish spatial coordinates that induces axis formation. Complex with tsu is essential for cytoplasmic localization of oskar in the posterior pole of oocytes. Required for the polarization of the oocyte microtubule cytoskeleton.[3] [4] [5] [6] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedY14 and Mago are conserved eukaryotic proteins that associate with spliced mRNAs in the nucleus and remain associated at exon junctions during and after nuclear export. In the cytoplasm, Y14 is involved in mRNA quality control via the nonsense-mediated mRNA decay (NMD) pathway and, together with Mago, is involved in localization of osk (oskar) mRNA. We have determined the crystal structure of the complex between Drosophila melanogaster Y14 and Mago at a resolution of 2.5 A. The structure reveals an atypical mode of protein-protein recognition mediated by an RNA-binding domain (RBD). Instead of binding RNA, the RBD of Y14 engages its RNP1 and RNP2 motifs to bind Mago. Using structure-guided mutagenesis, we show that Mago is also a component of the NMD pathway, and that its association with Y14 is essential for function. Heterodimerization creates a single structural platform that interacts with the NMD machinery via phylogenetically conserved residues. A novel mode of RBD-protein recognition in the Y14-Mago complex.,Fribourg S, Gatfield D, Izaurralde E, Conti E Nat Struct Biol. 2003 Jun;10(6):433-9. PMID:12730685[7] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||