You are hereBiblio / A model for histone H5-DNA interaction: simultaneous minor and major groove binding

A model for histone H5-DNA interaction: simultaneous minor and major groove binding

Publication Type:

Journal Article

Authors:

Segers,A.; Wyns,L.; Lasters,I.

Source:

Volume 174, Issue 2, p.898 - 902 (1991)

URL:

PM:1847057

Keywords:

Amino Acid Sequence; Cyclic AMP Receptor Protein; metabolism; Dna; chemistry; Escherichia coli; Histones; Models; Molecular; Molecular Sequence Data; Nucleic Acid Conformation; Protein Conformation; Sequence Homology; Nucleic Acid

Abstract:

Using the tertiary structure of the globular domain of H5 (GH5) and based on an alternative sequence homology between GH5 and DNA-binding proteins containing the helix-turn-helix motif, a model for H5-DNA interaction is proposed. From molecular graphics it follows that helix II recognizes the major groove of the DNA, as does the second helix of the helix-turn-helix motif, while helix III makes minor groove contacts, in agreement with the hypothesis of Turnell et al. (FEBS letters 232, 263-268). In the resulting model GH5 makes contact with a full turn of DNA

Notes:

DA - 19910308
IS - 0006-291X (Print)
LA - eng
PT - Comparative Study
PT - Journal Article
RN - 0 (Cyclic AMP Receptor Protein)
RN - 0 (Histones)
RN - 9007-49-2 (DNA)
SB - IM