1DU6
SOLUTION STRUCTURE OF THE TRUNCATED PBX HOMEODOMAIN
Summary for 1DU6
| Entry DOI | 10.2210/pdb1du6/pdb |
| Descriptor | HOMEOBOX PROTEIN PBX1 (1 entity in total) |
| Functional Keywords | homeodomain, gene regulation |
| Biological source | Mus musculus (house mouse) |
| Cellular location | Nucleus: P41778 |
| Total number of polymer chains | 1 |
| Total formula weight | 7458.35 |
| Authors | Sprules, T.,Green, N.,Featherstone, M.,Gehring, K. (deposition date: 2000-01-14, release date: 2000-08-16, Last modification date: 2024-05-22) |
| Primary citation | Sprules, T.,Green, N.,Featherstone, M.,Gehring, K. Conformational changes in the PBX homeodomain and C-terminal extension upon binding DNA and HOX-derived YPWM peptides. Biochemistry, 39:9943-9950, 2000 Cited by PubMed Abstract: PBX is a member of the three amino acid loop extension (TALE) class of homeodomains. PBX binds DNA cooperatively with HOX homeodomain proteins that contain a conserved YPWM motif. The amino acids immediately C-terminal to the PBX homeodomain increase the affinity of the homeodomain for its DNA site and HOX proteins. We have determined the structure of the free PBX homeodomain using NMR spectroscopy. Both the PBX homeodomain and the extended PBX homeodomain make identical contacts with a 5'-TGAT-3' DNA site and a YPWM peptide. A fourth alpha-helix, which forms upon binding to DNA, stabilizes the extended PBX structure. Variations in DNA sequence selectivity of heterodimeric PBX-HOX complexes depend on the HOX partner; however, a comparison of five different HOX-derived YPWM peptides showed that each bound to PBX in the same way, differing only in the strength of the association. PubMed: 10933814DOI: 10.1021/bi0001067 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
