1hu3: Difference between revisions

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==MIDDLE DOMAIN OF HUMAN EIF4GII==
==MIDDLE DOMAIN OF HUMAN EIF4GII==
<StructureSection load='1hu3' size='340' side='right'caption='[[1hu3]], [[Resolution|resolution]] 2.37&Aring;' scene=''>
<StructureSection load='1hu3' size='340' side='right'caption='[[1hu3]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<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>
<table><tr><td colspan='2'>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 [https://proteopedia.org/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>
</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=1hu3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hu3 OCA], [https://pdbe.org/1hu3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hu3 RCSB], [https://www.ebi.ac.uk/pdbsum/1hu3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hu3 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=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>
</table>
</table>
== 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> 
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=1hu3 ConSurf].
</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=1hu3 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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>
</div>
<div class="pdbe-citations 1hu3" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Eukaryotic initiation factor 3D structures|Eukaryotic initiation factor 3D structures]]
*[[Eukaryotic initiation factor 3D structures|Eukaryotic initiation factor 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Burley, S K]]
[[Category: Burley SK]]
[[Category: Hellen, C U.T]]
[[Category: Hellen CUT]]
[[Category: Lomakin, I]]
[[Category: Lomakin I]]
[[Category: Marcotrigiano, J]]
[[Category: Marcotrigiano J]]
[[Category: Pestova, T V]]
[[Category: Pestova TV]]
[[Category: Sonenberg, N]]
[[Category: Sonenberg N]]
[[Category: Eif4g]]
[[Category: Heat repeat]]
[[Category: Translation]]