2A3J
Structure of URNdesign, a complete computational redesign of human U1A protein
Summary for 2A3J
| Entry DOI | 10.2210/pdb2a3j/pdb |
| NMR Information | BMRB: 6493 |
| Descriptor | U1 small nuclear ribonucleoprotein A (1 entity in total) |
| Functional Keywords | computationally designed protein, rrm, u1a, rna binding protein |
| Biological source | Homo sapiens (human) |
| Cellular location | Nucleus: P09012 |
| Total number of polymer chains | 1 |
| Total formula weight | 13948.34 |
| Authors | Varani, G.,Dobson, N.,Dantas, G.,Baker, D. (deposition date: 2005-06-24, release date: 2006-06-06, Last modification date: 2024-05-22) |
| Primary citation | Dobson, N.,Dantas, G.,Baker, D.,Varani, G. High-Resolution Structural Validation of the Computational Redesign of Human U1A Protein Structure, 14:847-856, 2006 Cited by PubMed Abstract: Achieving atomic-level resolution in the computational design of a protein structure remains a challenging problem despite recent progress. Rigorous experimental tests are needed to improve protein design algorithms, yet studies of the structure and dynamics of computationally designed proteins are very few. The NMR structure and backbone dynamics of a redesigned protein of 96 amino acids are compared here with the design target, human U1A protein. We demonstrate that the redesigned protein reproduces the target structure to within the uncertainty of the NMR coordinates, even as 65 out of 96 amino acids were simultaneously changed by purely computational methods. The dynamics of the backbone of the redesigned protein also mirror those of human U1A, suggesting that the protein design algorithm captures the shape of the potential energy landscape in addition to the local energy minimum. PubMed: 16698546DOI: 10.1016/j.str.2006.02.011 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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