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. 1993 Jul 25;21(15):3427–3436. doi: 10.1093/nar/21.15.3427

Solution structure of a DNA-binding domain from HMG1.

C M Read 1, P D Cary 1, C Crane-Robinson 1, P C Driscoll 1, D G Norman 1
PMCID: PMC331441  PMID: 8346022

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.

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Selected References

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