Nucleic Acids Research, 1993, Vol. 21, No. 15 3427-3436
© 1993
STRUCTURAL BIOLOGY |
Solution structure of a DNA-binding domain from HMG1
Biophysics Laboratories, School of Biological Sciences, University of Portsmouth, Portsmouth PO1 2DT UK 1Department of Biochemistry, University of Oxford Oxford OX1 3QU, UK
*To whom correspondence should be addressed
Received April 30, 1993. Revised June 15, 1993. Accepted June 15, 1993.
We have determined the tertiary structure of box 2 from hamster HMG1 using bacterial expression and 3D NMR. The all ß-helical fold is in the form of a V-shaped arrowhead with helices along two edges and one rather flat face. This architecture is not related to any of the known DNA binding motifs. Inspection of the fold shows that the majority of conserved residue positions in the HMG box family are those involved in maintaining the tertiary structure and thus all homologous HMG boxes probably have essentially the same fold. Knowledge of the tertiary structure permits an interpretation of the mutations in HMG boxes known to abrogate DNA binding and suggests a mode of interaction with bent and 4-way junction DNA.
+Present address: Department of Biochemistry, University of Dundee, Dundee DD1 4HN, UK
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