NMR studies of the R2 repeat and related peptide fragments of the DNA binding domain of c-Myb. New light on the structure and folding of R2

Citation
I. Segalas et al., NMR studies of the R2 repeat and related peptide fragments of the DNA binding domain of c-Myb. New light on the structure and folding of R2, J CHIM PHYS, 96(9-10), 1999, pp. 1580-1584
Citations number
8
Categorie Soggetti
Physical Chemistry/Chemical Physics
Volume
96
Issue
9-10
Year of publication
1999
Pages
1580 - 1584
Database
ISI
SICI code
Abstract
The solution structure of the R2 repeat of the DNA binding domain of the pr otooncogene c-Myb contains a N-terminal structural motif comprising two ant iparallel helices. The motif is stabilized by interactions involving conser ved residues. The recognition region in C-terminal position is flexible. Th is structure differs from that of R2 of another c-Myb protein.