Solution structure of a DNA-binding domain from HMG1

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

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


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


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