1B72

PBX1, HOMEOBOX PROTEIN HOX-B1/DNA TERNARY COMPLEX

Summary for 1B72

• Entry DOI: 10.2210/pdb1b72/pdb
• Descriptor: DNA (5'-D(*AP*CP*TP*CP*TP*AP*TP*GP*AP*TP*TP*GP*AP*TP*CP*GP*GP*CP*TP*G)-3'), DNA (5'-D(*TP*CP*AP*GP*CP*CP*GP*AP*TP*CP*AP*AP*TP*CP*AP*TP*AP*GP*AP*G)-3'), PROTEIN (HOMEOBOX PROTEIN HOX-B1), ... (5 entities in total)
• Functional Keywords: homeodomain, dna, complex, dna-binding protein, protein-dna complex, protein/dna
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus: P14653; Nucleus (Probable): P40424
• Total number of polymer chains: 4
• Total formula weight: 33783.44

Authors

Piper, D.E.,Batchelor, A.H.,Chang, C.-P.,Cleary, M.L.,Wolberger, C. (deposition date: 1999-01-27, release date: 1999-02-19, Last modification date: 2023-12-27)

Primary citation

Piper, D.E.,Batchelor, A.H.,Chang, C.P.,Cleary, M.L.,Wolberger, C.
Structure of a HoxB1-Pbx1 heterodimer bound to DNA: role of the hexapeptide and a fourth homeodomain helix in complex formation.
Cell(Cambridge,Mass.), 96:587-597, 1999

PubMed 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.

PubMed: 10052460
DOI: 10.1016/S0092-8674(00)80662-5

Experimental method

X-RAY DIFFRACTION (2.35 Å)