1hmf
From Proteopedia
(New page: 200px<br /><applet load="1hmf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hmf" /> '''STRUCTURE OF THE HMG BOX MOTIF IN THE B-DOMA...) |
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| - | [[Image:1hmf.gif|left|200px]]<br /><applet load="1hmf" size=" | + | [[Image:1hmf.gif|left|200px]]<br /><applet load="1hmf" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1hmf" /> | caption="1hmf" /> | ||
'''STRUCTURE OF THE HMG BOX MOTIF IN THE B-DOMAIN OF HMG1'''<br /> | '''STRUCTURE OF THE HMG BOX MOTIF IN THE B-DOMAIN OF HMG1'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The conserved, abundant chromosomal protein HMG1 consists of two highly | + | 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== | ==About this Structure== | ||
| - | 1HMF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http:// | + | 1HMF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HMF OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Hill, C | + | [[Category: Hill, C S.]] |
| - | [[Category: Kraulis, P | + | [[Category: Kraulis, P J.]] |
| - | [[Category: Laue, E | + | [[Category: Laue, E D.]] |
| - | [[Category: Raine, A | + | [[Category: Raine, A R.C.]] |
| - | [[Category: Thomas, J | + | [[Category: Thomas, J O.]] |
| - | [[Category: Weir, H | + | [[Category: Weir, H M.]] |
[[Category: dna-binding]] | [[Category: dna-binding]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:02:44 2008'' |
Revision as of 11:02, 21 February 2008
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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
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