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| | ==Human eRF1 C-domain, "open" conformer== | | ==Human eRF1 C-domain, "open" conformer== |
| - | <StructureSection load='2ktv' size='340' side='right'caption='[[2ktv]], [[NMR_Ensembles_of_Models | 24 NMR models]]' scene=''> | + | <StructureSection load='2ktv' size='340' side='right'caption='[[2ktv]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2ktv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KTV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KTV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2ktv]] 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=2KTV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KTV FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2hst|2hst]], [[1dt9|1dt9]], [[2ktu|2ktu]]</div></td></tr> | + | </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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ETF1, ERF1, RF1, SUP45L1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ktv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ktv OCA], [https://pdbe.org/2ktv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ktv RCSB], [https://www.ebi.ac.uk/pdbsum/2ktv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ktv 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=2ktv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ktv OCA], [https://pdbe.org/2ktv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ktv RCSB], [https://www.ebi.ac.uk/pdbsum/2ktv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ktv ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == 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>
| + | [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> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Birdsall, B]] | + | [[Category: Birdsall B]] |
| - | [[Category: Mantsyzov, A B]] | + | [[Category: Mantsyzov AB]] |
| - | [[Category: Polshakov, V I]] | + | [[Category: Polshakov VI]] |
| - | [[Category: C domain]]
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| - | [[Category: Erf1]]
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| - | [[Category: Eukaryote]]
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| - | [[Category: Protein biosynthesis]]
| + | |
| - | [[Category: Termination]]
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| - | [[Category: Translation]]
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| Structural highlights
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]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Termination of translation in eukaryotes is triggered by two polypeptide chain release factors, eukaryotic class 1 polypeptide chain release factor (eRF1) and eukaryotic class 2 polypeptide chain release factor 3. eRF1 is a three-domain protein that interacts with eukaryotic class 2 polypeptide chain release factor 3 via its C-terminal domain (C-domain). The high-resolution NMR structure of the human C-domain (residues 277-437) has been determined in solution. The overall fold and the structure of the beta-strand core of the protein in solution are similar to those found in the crystal structure. The structure of the minidomain (residues 329-372), which was ill-defined in the crystal structure, has been determined in solution. The protein backbone dynamics, studied using (15)N-relaxation experiments, showed that the C-terminal tail 414-437 and the minidomain are the most flexible parts of the human C-domain. The minidomain exists in solution in two conformational states, slowly interconverting on the NMR timescale. Superposition of this NMR solution structure of the human C-domain onto the available crystal structure of full-length human eRF1 shows that the minidomain is close to the stop codon-recognizing N-terminal domain. Mutations in the tip of the minidomain were found to affect the stop codon specificity of the factor. The results provide new insights into the possible role of the C-domain in the process of translation termination.
NMR solution structure and function of the C-terminal domain of eukaryotic class 1 polypeptide chain release factor.,Mantsyzov AB, Ivanova EV, Birdsall B, Alkalaeva EZ, Kryuchkova PN, Kelly G, Frolova LY, Polshakov VI FEBS J. 2010 Jun;277(12):2611-27. PMID:20553496[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
- ↑ Mantsyzov AB, Ivanova EV, Birdsall B, Alkalaeva EZ, Kryuchkova PN, Kelly G, Frolova LY, Polshakov VI. NMR solution structure and function of the C-terminal domain of eukaryotic class 1 polypeptide chain release factor. FEBS J. 2010 Jun;277(12):2611-27. PMID:20553496 doi:10.1111/j.1742-464X.2010.07672.x
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