A DNA-binding homeodomain in histone H1.
The structure of the globular domain of chicken histone H1 was compared here with that of the DNA-binding homeodomain in the Drosophila Antp protein, and they were observed to display considerable similarity. Both of them consist of three or four alpha-helices separated by well-defined turns. Charged residues in the aminoterminal end of alpha 3 are therefore suggested to be responsible for sequence-specific recognition of DNA by the histone. In addition, alpha 2 of H1, with a short leucine zipper in it, may be capable of protein-protein interaction in a similar manner to the other homeodomains.
Mannermaa
R M
RM
Collagen Research Unit, University of Oulu, Finland.
Oikarinen
J
J
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002645:Chickens; D004268:DNA-Binding Proteins / Q000378:metabolism* / Q000648:ultrastructure; D006657:Histones / Q000378:metabolism* / Q000648:ultrastructure; D008969:Molecular Sequence Data; D011487:Protein Conformation; D012995:Solubility
D004268:DNA-Binding Proteins; D006657:Histones