Abstract：
:Hox homeodomain proteins are developmental regulators that determine body plan in a variety of organisms. A majority of the vertebrate Hox proteins bind DNA as heterodimers with the Pbx1 homeodomain protein. We report here the 2.35 A structure of a ternary complex containing a human HoxB1-Pbx1 heterodimer bound to DNA. Heterodimer contacts are mediated by the hexapeptide of HoxB1, which binds in a pocket in the Pbx1 protein formed in part by a three-amino acid insertion in the Pbx1 homeodomain. The Pbx1 DNA-binding domain is larger than the canonical homeodomain, containing an additional alpha helix that appears to contribute to binding of the HoxB1 hexapeptide and to stable binding of Pbx1 to DNA. The structure suggests a model for modulation of Hox DNA binding activity by Pbx1 and related proteins.
journal_name
Celljournal_title
Cellauthors
Piper DE,Batchelor AH,Chang CP,Cleary ML,Wolberger Cdoi
10.1016/s0092-8674(00)80662-5subject
Has Abstractpub_date
1999-02-19 00:00:00pages
587-97issue
4eissn
0092-8674issn
1097-4172pii
S0092-8674(00)80662-5journal_volume
96pub_type
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