Solution structure of a DNA-binding domain from HMG1
Year: 1993
Type: article
Abstract: We have determined the tertiary structure of box 2 from hamster HMG1 using bacterial expression and 3D NMR. The all alpha-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.
Source: Nucleic Acids Research
Authors: Christopher M. Read, Peter D. Cary, Colyn Crane-Robinson, Paul C. Driscoll, David G. Norman
Institutions: University of Portsmouth, University of Oxford
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: green
Funder: Wellcome Trust
OpenAlex ID: W2022689945