Solution structure of a DNA-binding domain from HMG1

Christopher M. Read, Peter D. Cary, Colyn Crane-robinson, Paul C. Driscoll, David G. Norman

    Research output: Contribution to journalArticlepeer-review

    258 Citations (Scopus)


    We have determined the tertiary structure of box 2 from hamster HMG1 using bacterial expression and 3D NMR. The all β-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.

    Original languageEnglish
    Pages (from-to)3427-3436
    Number of pages10
    JournalNucleic Acids Research
    Issue number15
    Publication statusPublished - 25 Jul 1993

    ASJC Scopus subject areas

    • Genetics


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