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2llx

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Revision as of 20:00, 1 August 2018

Solution structure of the N-terminal domain of human polypeptide chain release factor eRF1

Structural highlights

2llx is a 1 chain structure with sequence from Human. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1dt9, 3e1y, 2hst, 2ktv, 2ktu
Gene:	ETF1, ERF1, RF1, SUP45L1 (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1]

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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Frolova L, Le Goff X, Rasmussen HH, Cheperegin S, Drugeon G, Kress M, Arman I, Haenni AL, Celis JE, Philippe M, et al.. A highly conserved eukaryotic protein family possessing properties of polypeptide chain release factor. Nature. 1994 Dec 15;372(6507):701-3. PMID:7990965 doi:http://dx.doi.org/10.1038/372701a0
↑ Polshakov VI, Eliseev BD, Birdsall B, Frolova LY. Structure and dynamics in solution of the stop codon decoding N-terminal domain of the human polypeptide chain release factor eRF1. Protein Sci. 2012 Jun;21(6):896-903. doi: 10.1002/pro.2067. Epub 2012 Apr 19. PMID:22517631 doi:10.1002/pro.2067

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2llx"

@@ Line 1: / Line 1: @@
 ==Solution structure of the N-terminal domain of human polypeptide chain release factor eRF1==
 <StructureSection load='2llx' size='340' side='right' caption='[[2llx]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1dt9|1dt9]], [[3e1y|3e1y]], [[2hst|2hst]], [[2ktv|2ktv]], [[2ktu|2ktu]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ETF1, ERF1, RF1, SUP45L1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=2llx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2llx OCA], [http://pdbe.org/2llx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2llx RCSB], [http://www.ebi.ac.uk/pdbsum/2llx PDBsum]</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=2llx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2llx OCA], [http://pdbe.org/2llx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2llx RCSB], [http://www.ebi.ac.uk/pdbsum/2llx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2llx ProSAT]</span></td></tr>
 </table>
 == Function ==

2llx

From Proteopedia

Revision as of 20:00, 1 August 2018

Solution structure of the N-terminal domain of human polypeptide chain release factor eRF1

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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