4uec: Difference between revisions
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==Complex of D. melanogaster eIF4E with eIF4G and cap analog== | ==Complex of D. melanogaster eIF4E with eIF4G and cap analog== | ||
<StructureSection load='4uec' size='340' side='right' caption='[[4uec]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='4uec' size='340' side='right' caption='[[4uec]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MGT:7N-METHYL-8-HYDROGUANOSINE-5-TRIPHOSPHATE'>MGT</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MGT:7N-METHYL-8-HYDROGUANOSINE-5-TRIPHOSPHATE'>MGT</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ue8|4ue8]], [[4ue9|4ue9]], [[4uea|4uea]], [[4ueb|4ueb]], [[4ued|4ued]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ue8|4ue8]], [[4ue9|4ue9]], [[4uea|4uea]], [[4ueb|4ueb]], [[4ued|4ued]]</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=4uec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uec OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4uec RCSB], [http://www.ebi.ac.uk/pdbsum/4uec PDBsum]</span></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=4uec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uec OCA], [http://pdbe.org/4uec PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4uec RCSB], [http://www.ebi.ac.uk/pdbsum/4uec PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4uec ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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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 4uec" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
Revision as of 04:10, 19 January 2017
Complex of D. melanogaster eIF4E with eIF4G and cap analogComplex of D. melanogaster eIF4E with eIF4G and cap analog
Structural highlights
Function[IF4E_DROME] Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures.[1] Publication Abstract from PubMedThe eIF4E-binding proteins (4E-BPs) represent a diverse class of translation inhibitors that are often deregulated in cancer cells. 4E-BPs inhibit translation by competing with eIF4G for binding to eIF4E through an interface that consists of canonical and non-canonical eIF4E-binding motifs connected by a linker. The lack of high-resolution structures including the linkers, which contain phosphorylation sites, limits our understanding of how phosphorylation inhibits complex formation. Furthermore, the binding mechanism of the non-canonical motifs is poorly understood. Here, we present structures of human eIF4E bound to 4E-BP1 and fly eIF4E bound to Thor, 4E-T, and eIF4G. These structures reveal architectural elements that are unique to 4E-BPs and provide insight into the consequences of phosphorylation. Guided by these structures, we designed and crystallized a 4E-BP mimic that shows increased repressive activity. Our studies pave the way for the rational design of 4E-BP mimics as therapeutic tools to decrease translation during oncogenic transformation. Molecular Architecture of 4E-BP Translational Inhibitors Bound to eIF4E.,Peter D, Igreja C, Weber R, Wohlbold L, Weiler C, Ebertsch L, Weichenrieder O, Izaurralde E Mol Cell. 2015 Feb 18. pii: S1097-2765(15)00018-0. doi:, 10.1016/j.molcel.2015.01.017. PMID:25702871[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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