2p6j

Full-sequence computational design and solution structure of a thermostable protein variantFull-sequence computational design and solution structure of a thermostable protein variant

Structural highlights 2p6j is a 1 chain structure with sequence from Unidentified. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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. Full-sequence computational design and solution structure of a thermostable protein variant.,Shah PS, Hom GK, Ross SA, Lassila JK, Crowhurst KA, Mayo SL J Mol Biol. 2007 Sep 7;372(1):1-6. Epub 2007 Jun 16. PMID:17628593 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 2p6j Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image