1hmf
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1hmf.gif|left|200px]] | [[Image:1hmf.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1hmf", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | | | + | or leave the SCENE parameter empty for the default display. |
| - | | | + | --> |
| - | + | {{STRUCTURE_1hmf| PDB=1hmf | SCENE= }} | |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''STRUCTURE OF THE HMG BOX MOTIF IN THE B-DOMAIN OF HMG1''' | '''STRUCTURE OF THE HMG BOX MOTIF IN THE B-DOMAIN OF HMG1''' | ||
| Line 31: | Line 28: | ||
[[Category: Thomas, J O.]] | [[Category: Thomas, J O.]] | ||
[[Category: Weir, H M.]] | [[Category: Weir, H M.]] | ||
| - | [[Category: | + | [[Category: Dna-binding]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:00:55 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 16:00, 2 May 2008
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 Fri May 2 19:00:55 2008
