View source for 2llx


==Solution structure of the N-terminal domain of human polypeptide chain release factor eRF1==
<StructureSection load='2llx' size='340' side='right'caption='[[2llx]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2llx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LLX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LLX FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2llx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2llx OCA], [https://pdbe.org/2llx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2llx RCSB], [https://www.ebi.ac.uk/pdbsum/2llx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2llx ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ERF1_HUMAN ERF1_HUMAN] Directs the termination of nascent peptide synthesis (translation) in response to the termination codons UAA, UAG and UGA. Component of the transient SURF complex which recruits UPF1 to stalled ribosomes in the context of nonsense-mediated decay (NMD) of mRNAs containing premature stop codons.<ref>PMID:7990965</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The high-resolution NMR structure of the N-domain of human eRF1, responsible for stop codon recognition, has been determined in solution. The overall fold of the protein is the same as that found in the crystal structure. However, the structures of several loops, including those participating in stop codon decoding, are different. Analysis of the NMR relaxation data reveals that most of the regions with the highest structural discrepancy between the solution and solid states undergo internal motions on the ps-ns and ms time scales. The NMR data show that the N-domain of human eRF1 exists in two conformational states. The distribution of the residues having the largest chemical shift differences between the two forms indicates that helices alpha2 and alpha3, with the NIKS loop between them, can switch their orientation relative to the beta-core of the protein. Such structural plasticity may be essential for stop codon recognition by human eRF1.

Structure and dynamics in solution of the stop codon decoding N-terminal domain of the human polypeptide chain release factor eRF1.,Polshakov VI, Eliseev BD, Birdsall B, Frolova LY Protein Sci. 2012 Jun;21(6):896-903. doi: 10.1002/pro.2067. Epub 2012 Apr 19. PMID:22517631<ref>PMID:22517631</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2llx" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Birdsall B]]
[[Category: Eliseev BD]]
[[Category: Frolova LY]]
[[Category: Polshakov VI]]