2P6J
Full-sequence computational design and solution structure of a thermostable protein variant
Summary for 2P6J
| Entry DOI | 10.2210/pdb2p6j/pdb |
| NMR Information | BMRB: 7401 |
| Descriptor | designed engrailed homeodomain variant UVF (1 entity in total) |
| Functional Keywords | de novo protein, helix-turn-helix, computational protein design, engrailed homeodomain |
| Biological source | unidentified |
| Total number of polymer chains | 1 |
| Total formula weight | 6605.41 |
| Authors | Shah, P.S.,Hom, G.K.,Ross, S.A.,Lassila, J.K.,Crowhurst, K.A.,Mayo, S.L. (deposition date: 2007-03-18, release date: 2007-08-14, Last modification date: 2024-05-22) |
| Primary citation | Shah, P.S.,Hom, G.K.,Ross, S.A.,Lassila, J.K.,Crowhurst, K.A.,Mayo, S.L. Full-sequence Computational Design and Solution Structure of a Thermostable Protein Variant. J.Mol.Biol., 372:1-6, 2007 Cited by PubMed Abstract: Computational protein design procedures were applied to the redesign of the entire sequence of a 51 amino acid residue protein, Drosophila melanogaster engrailed homeodomain. Various sequence optimization algorithms were compared and two resulting designed sequences were experimentally evaluated. The two sequences differ by 11 mutations and share 22% and 24% sequence identity with the wild-type protein. Both computationally designed proteins were considerably more stable than the naturally occurring protein, with midpoints of thermal denaturation greater than 99 degrees C. The solution structure was determined for one of the two sequences using multidimensional heteronuclear NMR spectroscopy, and the structure was found to closely match the original design template scaffold. PubMed: 17628593DOI: 10.1016/j.jmb.2007.06.032 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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