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High resolution NMR solution structure of the M-domain of human eRF1 has been determined and deposited to PDB under accession code 2HST. Overall topology of the protein is similar to the crystal structure with the most evident differences in the loop 177–187. Representative conformation of the mobile GGQ loop has been obtained. Change of protein conformation upon the functionally fatal G183A mutation of the M-domain of human eRF1 was not detected. Backbone amide protons in the loop 177–187 of the M-domain of human eRF1 undergo fast exchange with water. G183A mutation significantly decrease the exchange rates of amide protons with water in the GGQ loop. Protein backbone motions in fast (ps to ns) and slow (ms) time scales were studied using the NMR relaxation measurements. Three regions of the M-domain are mobile in fast time scale: N-terminal residues, GGQ loop and loop between helix 1 and strand 5. There are also several regions of the protein backbone that exhibit conformational rearrangements occurring in the ms time scale.