2p6j

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2p6j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p6j OCA], [http://www.ebi.ac.uk/pdbsum/2p6j PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2p6j RCSB]</span>
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Revision as of 01:30, 31 March 2008


PDB ID 2p6j

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Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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


Overview

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.

About this Structure

2P6J is a Protein complex structure of sequences from Unidentified. Full crystallographic information is available from OCA.

Reference

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

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