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ADR1a, a zinc finger peptide, exists in two folded conformations

Journal Article · · Biochemistry; (United States)
DOI:https://doi.org/10.1021/bi00228a003· OSTI ID:5595082
;  [1];  [2]
  1. Univ. of Washington, Seattle (USA)
  2. California Inst. of Tech., Pasadena (USA)
Two-dimensional NMR (2DNMR) studies of several different zinc finger peptides have yielded a picture of the three-dimensional structure of this small DNA-binding motif. Details of the differences among fingers with different sequences may provide some insight into how these domains interact with DNA. Toward this end, the authors have reanalyzed the 2DNMR spectra of the C-terminal zinc finger sequences from the yeast transcriptional factor ADR1. Although this was the sequence on which the original report describing the overall fold of zinc fingers was based, complete spectral assignments were needed to compare this sequence in detail with that of ADR1b, for which they have reported an atomic level structure. In the process of analyzing the spectra of ADR1a and a mutant of ADR1a, it was noted that the peptides give two sets of NMR lines, indicating that this sequence, unlike the other ADR1 zinc finger sequence, exists in two slowly interconverting folded conformations in solution. Residues that exhibit peak doubling are located in the Cys loop, the {alpha}-helix, and the extreme C-terminus of the peptide. Differences in NOEs observed for the two forms indicate that there are detectable conformational differences in the Zn{sup 2+} cluster and in the fingertip region. This conformational flexibility, which has not been observed for other zinc finger peptides, may stem from the presence of an additional residue between the histidine ligands.
OSTI ID:
5595082
Journal Information:
Biochemistry; (United States), Journal Name: Biochemistry; (United States) Vol. 30:14; ISSN 0006-2960; ISSN BICHA
Country of Publication:
United States
Language:
English

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