4ueb: Difference between revisions
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==Complex of D. melanogaster eIF4E with a designed 4E-binding protein (Form II)== | ==Complex of D. melanogaster eIF4E with a designed 4E-binding protein (Form II)== | ||
<StructureSection load='4ueb' size='340' side='right' caption='[[4ueb]], [[Resolution|resolution]] 2.52Å' scene=''> | <StructureSection load='4ueb' size='340' side='right'caption='[[4ueb]], [[Resolution|resolution]] 2.52Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4ueb]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UEB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UEB FirstGlance]. <br> | <table><tr><td colspan='2'>[[4ueb]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome] and [http://en.wikipedia.org/wiki/Synthetic_construct_sequences Synthetic construct sequences]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UEB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UEB FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ue8|4ue8]], [[4ue9|4ue9]], [[4uea|4uea]], [[4uec|4uec]], [[4ued|4ued]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ue8|4ue8]], [[4ue9|4ue9]], [[4uea|4uea]], [[4uec|4uec]], [[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=4ueb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ueb OCA], [http://pdbe.org/4ueb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ueb RCSB], [http://www.ebi.ac.uk/pdbsum/4ueb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ueb ProSAT]</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=4ueb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ueb OCA], [http://pdbe.org/4ueb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ueb RCSB], [http://www.ebi.ac.uk/pdbsum/4ueb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ueb ProSAT]</span></td></tr> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Drome]] | |||
[[Category: Large Structures]] | |||
[[Category: Synthetic construct sequences]] | |||
[[Category: Peter, D]] | [[Category: Peter, D]] | ||
[[Category: Weichenrieder, O]] | [[Category: Weichenrieder, O]] | ||
Revision as of 12:12, 21 May 2019
Complex of D. melanogaster eIF4E with a designed 4E-binding protein (Form II)Complex of D. melanogaster eIF4E with a designed 4E-binding protein (Form II)
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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