1MBF
MOUSE C-MYB DNA-BINDING DOMAIN REPEAT 1
Summary for 1MBF
| Entry DOI | 10.2210/pdb1mbf/pdb |
| Descriptor | MYB PROTO-ONCOGENE PROTEIN (1 entity in total) |
| Functional Keywords | protooncogene product, dna binding protein |
| Biological source | Mus musculus (house mouse) |
| Cellular location | Nucleus: P06876 |
| Total number of polymer chains | 1 |
| Total formula weight | 6317.11 |
| Authors | Ogata, K.,Morikawa, S.,Nakamura, H.,Hojo, H.,Yoshimura, S.,Zhang, R.,Aimoto, S.,Ametani, Y.,Hirata, Z.,Sarai, A.,Ishii, S.,Nishimura, Y. (deposition date: 1995-05-19, release date: 1995-07-31, Last modification date: 2024-10-16) |
| Primary citation | Ogata, K.,Morikawa, S.,Nakamura, H.,Hojo, H.,Yoshimura, S.,Zhang, R.,Aimoto, S.,Ametani, Y.,Hirata, Z.,Sarai, A.,Ishii, S.,Nishimura, Y. Comparison of the free and DNA-complexed forms of the DNA-binding domain from c-Myb. Nat.Struct.Biol., 2:309-320, 1995 Cited by PubMed Abstract: The DNA-binding domain of c-Myb consists of three imperfect tandem repeats (R1, R2 and R3). The three repeats have similar overall architectures, each containing a helix-turn-helix variation motif. The three conserved tryptophans in each repeat participate in forming a hydrophobic core. Comparison of the three repeat structures indicated that cavities are found in the hydrophobic core of R2, which is thermally unstable. On complexation with DNA, the orientations of R2 and R3 are fixed by tight binding and their conformations are slightly changed. No significant changes occur in the chemical shifts of R1 consistent with its loose interaction with DNA. PubMed: 7796266DOI: 10.1038/nsb0495-309 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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