1IDZ
STRUCTURE OF MYB TRANSFORMING PROTEIN, NMR, 20 STRUCTURES
Summary for 1IDZ
| Entry DOI | 10.2210/pdb1idz/pdb |
| Related | 1IDY |
| Descriptor | MOUSE C-MYB DNA-BINDING DOMAIN REPEAT 3 (1 entity in total) |
| Functional Keywords | protooncogene product, dna-binding protein, dna binding protein |
| Biological source | Mus musculus (house mouse) |
| Cellular location | Nucleus: P06876 |
| Total number of polymer chains | 1 |
| Total formula weight | 6521.50 |
| Authors | Furukawa, K.,Oda, M.,Nakamura, H. (deposition date: 1996-08-15, release date: 1996-12-23, Last modification date: 2024-05-22) |
| Primary citation | Furukawa, K.,Oda, M.,Nakamura, H. A small engineered protein lacks structural uniqueness by increasing the side-chain conformational entropy. Proc.Natl.Acad.Sci.USA, 93:13583-13588, 1996 Cited by PubMed Abstract: A small globular protein, the third repeat of the c-Myb DNA-binding domain, which is composed of 54 amino acid residues, was engineered so as to understand the structural uniqueness of native proteins. This small protein has three alpha-helices that form a helix-turn-helix structure, which is maintained by the hydrophobic core with three Ile residues. One of the mutant proteins, with two of the buried Ile (Ile-155 and Ile-181) substituted with Leu residues, showed multiple conformations, as monitored by heteronuclear magnetic resonance spectroscopy for 13C- and 15N-labeled proteins. The increase in the side-chain conformational entropy, caused by changing the Ile to a Leu residue on an alpha-helix, could engender the lack of structural uniqueness. In native proteins, the conformations of not only the beta-branched side chains, but also those of the neighboring bulky side chains, can be greatly restricted, depending upon the local backbone structure. PubMed: 8942977DOI: 10.1073/pnas.93.24.13583 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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