1hmf
From Proteopedia
|
STRUCTURE OF THE HMG BOX MOTIF IN THE B-DOMAIN OF HMG1
Overview
The conserved, abundant chromosomal protein HMG1 consists of two highly, homologous, folded, basic DNA-binding domains, each of approximately 80, amino acid residues, and an acidic C-terminal tail. Each folded domain, represents an 'HMG box', a sequence motif recently recognized in certain, sequence-specific DNA-binding proteins and which also occurs in abundant, HMG1-like proteins that bind to DNA without sequence specificity. The HMG, box is defined by a set of highly conserved residues (most distinctively, aromatic and basic) and appears to define a novel DNA-binding structural, motif. We have expressed the HMG box region of the B-domain of rat HMG1, (residues 88-164 of the intact protein) in Escherichia coli and we, describe here the determination of its structure by 2D 1H-NMR, spectroscopy. There are three alpha-helices (residues 13-29, 34-48 and, 50-74), which together account for approximately 75% of the total residues, and contain many of the conserved basic and aromatic residues. Strikingly, the molecule is L-shaped, the angle of approximately 80 degrees between, the two arms being defined by a cluster of conserved, predominantly, aromatic, residues. The distinctive shape of the HMG box motif, which is, distinct from hitherto characterized DNA-binding motifs, may be, significant in relation to its recognition of four-way DNA junctions.
About this Structure
1HMF is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Structure of the HMG box motif in the B-domain of HMG1., Weir HM, Kraulis PJ, Hill CS, Raine AR, Laue ED, Thomas JO, EMBO J. 1993 Apr;12(4):1311-9. PMID:8467791
Page seeded by OCA on Tue Nov 20 16:39:18 2007
