1hu3

<StructureSection load='1hu3' size='340' side='right'caption='[[1hu3]], [[Resolution|resolution]] 2.37&Aring;' scene=''>

<table><tr><td colspan='2'>[[1hu3]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HU3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HU3 FirstGlance]. <br>

</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=1hu3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hu3 OCA], [http://pdbe.org/1hu3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hu3 RCSB], [http://www.ebi.ac.uk/pdbsum/1hu3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1hu3 ProSAT]</span></td></tr>

== Function ==

[[http://www.uniprot.org/uniprot/IF4G3_HUMAN IF4G3_HUMAN]] Probable component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome. Thought to be a functional homolog of EIF4G1.<ref>PMID:9418880</ref>

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== Publication Abstract from PubMed ==

The X-ray structure of the phylogenetically conserved middle portion of human eukaryotic initiation factor (eIF) 4GII has been determined at 2.4 A resolution, revealing a crescent-shaped domain consisting of ten alpha helices arranged as five HEAT repeats. Together with the ATP-dependent RNA helicase eIF4A, this HEAT domain suffices for 48S ribosomal complex formation with a picornaviral RNA internal ribosome entry site (IRES). Structure-based site-directed mutagenesis was used to identify two adjacent features on the surface of this essential component of the translation initiation machinery that, respectively, bind eIF4A and a picornaviral IRES. The structural and biochemical results provide mechanistic insights into both cap-dependent and cap-independent translation initiation.

A conserved HEAT domain within eIF4G directs assembly of the translation initiation machinery.,Marcotrigiano J, Lomakin IB, Sonenberg N, Pestova TV, Hellen CU, Burley SK Mol Cell. 2001 Jan;7(1):193-203. PMID:11172724<ref>PMID:11172724</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Burley, S K]]

[[Category: Hellen, C U.T]]

[[Category: Lomakin, I]]

[[Category: Marcotrigiano, J]]

[[Category: Pestova, T V]]

[[Category: Sonenberg, N]]

[[Category: Translation]]