1HME

STRUCTURE OF THE HMG BOX MOTIF IN THE B-DOMAIN OF HMG1

Summary for 1HME

• Entry DOI: 10.2210/pdb1hme/pdb
• Descriptor: HIGH MOBILITY GROUP PROTEIN FRAGMENT-B (1 entity in total)
• Functional Keywords: dna-binding
• Biological source: Rattus norvegicus (Norway rat)
• Cellular location: Nucleus: P63159
• Total number of polymer chains: 1
• Total formula weight: 8791.12

Authors

Weir, H.M.,Kraulis, P.J.,Hill, C.S.,Raine, A.R.C.,Laue, E.D.,Thomas, J.O. (deposition date: 1994-02-10, release date: 1994-05-31, Last modification date: 2024-05-22)

Primary citation

Weir, H.M.,Kraulis, P.J.,Hill, C.S.,Raine, A.R.,Laue, E.D.,Thomas, J.O.
Structure of the HMG box motif in the B-domain of HMG1.
EMBO J., 12:1311-1319, 1993

PubMed Abstract: 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.

PubMed: 8467791

Experimental method

SOLUTION NMR