2MYO
SOLUTION STRUCTURE OF MYOTROPHIN, NMR, MINIMIZED AVERAGE STRUCTURE
Summary for 2MYO
| Entry DOI | 10.2210/pdb2myo/pdb |
| Descriptor | MYOTROPHIN (1 entity in total) |
| Functional Keywords | myotrophin, acetylation, ank-repeat |
| Biological source | Rattus norvegicus (Norway rat) |
| Cellular location | Cytoplasm: P62775 |
| Total number of polymer chains | 1 |
| Total formula weight | 12878.77 |
| Authors | Yang, Y.,Nanduri, S.,Sen, S.,Qin, J. (deposition date: 1998-08-17, release date: 1999-08-17, Last modification date: 2024-05-22) |
| Primary citation | Yang, Y.,Nanduri, S.,Sen, S.,Qin, J. The structural basis of ankyrin-like repeat function as revealed by the solution structure of myotrophin. Structure, 6:619-626, 1998 Cited by PubMed Abstract: Myotrophin is a 12.5 kDa protein that appears to have a key role in the initiation of cardiac hypertrophy, a central process in many heart diseases. Myotrophin primarily comprises ankyrin-like (ANK) repeats, the 33 amino acid motifs involved in a wide range of protein-protein interactions. As a first step in the structure-based search for cardiac hypertrophy antagonists and in order to gain insight into the molecular basis of action of the ubiquitous and multifunctional ANK repeat motif, we have determined the solution structure of myotrophin using multidimensional heteronuclear NMR spectroscopy. PubMed: 9634699DOI: 10.1016/S0969-2126(98)00063-X PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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