Ontology highlight
ABSTRACT:
SUBMITTER: Polshakov VI
PROVIDER: S-EPMC3403424 | biostudies-literature | 2012 Jun
REPOSITORIES: biostudies-literature
Polshakov Vladimir I VI Eliseev Boris D BD Birdsall Berry B Frolova Ludmila Yu LY
Protein science : a publication of the Protein Society 20120419 6
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 mot ...[more]