5t48: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 3: / Line 3: @@
 <StructureSection load='5t48' size='340' side='right'caption='[[5t48]], [[Resolution|resolution]] 2.19&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5t48]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5T48 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5T48 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5t48]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5T48 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5T48 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MGP:7-METHYL-GUANOSINE-5-TRIPHOSPHATE'>MGP</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.19&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">eIF-4E, Eif4e, EIF4F, CG4035 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME]), eIF4G, eIF-4G, eIF4G-RA, CG10811, Dmel_CG10811 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MGP:7-METHYL-GUANOSINE-5-TRIPHOSPHATE'>MGP</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5t48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t48 OCA], [http://pdbe.org/5t48 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5t48 RCSB], [http://www.ebi.ac.uk/pdbsum/5t48 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5t48 ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5t48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t48 OCA], [https://pdbe.org/5t48 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5t48 RCSB], [https://www.ebi.ac.uk/pdbsum/5t48 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5t48 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/IF4E_DROME 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.<ref>PMID:8663200</ref>
+[https://www.uniprot.org/uniprot/IF4E_DROME 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.<ref>PMID:8663200</ref>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Eukaryotic initiation factor 4G (eIF4G) plays a central role in translation initiation through its interactions with the cap-binding protein eIF4E. This interaction is a major drug target for repressing translation and is naturally regulated by 4E-binding proteins (4E-BPs). 4E-BPs and eIF4G compete for binding to the eIF4E dorsal surface via a shared canonical 4E-binding motif, but also contain auxiliary eIF4E-binding sequences, which were assumed to contact non-overlapping eIF4E surfaces. However, it is unknown how metazoan eIF4G auxiliary sequences bind eIF4E. Here, we describe crystal structures of human and Drosophila melanogaster eIF4E-eIF4G complexes, which unexpectedly reveal that the eIF4G auxiliary sequences bind to the lateral surface of eIF4E, using a similar mode to that of 4E-BPs. Our studies provide a molecular model of the eIF4E-eIF4G complex, shed light on the competition mechanism of 4E-BPs, and enable the rational design of selective eIF4G inhibitors to dampen dysregulated translation in disease.
-The Structures of eIF4E-eIF4G Complexes Reveal an Extended Interface to Regulate Translation Initiation.,Gruner S, Peter D, Weber R, Wohlbold L, Chung MY, Weichenrieder O, Valkov E, Igreja C, Izaurralde E Mol Cell. 2016 Oct 19. pii: S1097-2765(16)30569-X. doi:, 10.1016/j.molcel.2016.09.020. PMID:27773676<ref>PMID:27773676</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 5t48" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 26: / Line 17: @@
 __TOC__
 </StructureSection>
-[[Category: Drome]]
+[[Category: Drosophila melanogaster]]
 [[Category: Large Structures]]
-[[Category: Chung, M Y]]
+[[Category: Chung M-Y]]
-[[Category: Gruener, S]]
+[[Category: Gruener S]]
-[[Category: Igreja, C]]
+[[Category: Igreja C]]
-[[Category: Izaurralde, E]]
+[[Category: Izaurralde E]]
-[[Category: Peter, D]]
+[[Category: Peter D]]
-[[Category: Valkov, E]]
+[[Category: Valkov E]]
-[[Category: Weber, R]]
+[[Category: Weber R]]
-[[Category: Weichenrieder, O]]
+[[Category: Weichenrieder O]]
-[[Category: Wohlbold, L]]
+[[Category: Wohlbold L]]
-[[Category: 4e-binding protein]]
-[[Category: Cap binding protein]]
-[[Category: Eif4f]]
-[[Category: Gene regulation]]
-[[Category: Translation]]
-[[Category: Translation initiation]]