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
We report NMR assignments of the protein backbone of the C-terminal domain (163 a.a.) of human class 1 translation termination factor eRF1. It was found that several protein loop residues exist in two slowly interconverting conformational states.
NMR assignments of the C-terminal domain of human polypeptide release factor eRF1.,Mantsyzov AB, Ivanova EV, Birdsall B, Kolosov PM, Kisselev LL, Polshakov VI Biomol NMR Assign. 2007 Dec;1(2):183-5. Epub 2007 Oct 30. PMID:19636860[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, Kolosov PM, Kisselev LL, Polshakov VI. NMR assignments of the C-terminal domain of human polypeptide release factor eRF1. Biomol NMR Assign. 2007 Dec;1(2):183-5. Epub 2007 Oct 30. PMID:19636860 doi:10.1007/s12104-007-9050-z