1zsz
From Proteopedia
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Crystal structure of a computationally designed SspB heterodimer
Overview
Protein-protein interactions can be designed computationally by using, positive strategies that maximize the stability of the desired structure, and/or by negative strategies that seek to destabilize competing states., Here, we compare the efficacy of these methods in reengineering a protein, homodimer into a heterodimer. The stability-design protein (positive, design only) was experimentally more stable than the specificity-design, heterodimer (positive and negative design). By contrast, only the, specificity-design protein assembled as a homogenous heterodimer in, solution, whereas the stability-design protein formed a mixture of, homodimer and heterodimer species. The experimental stabilities of the, engineered proteins correlated roughly with their calculated stabilities, and the crystal structure of the specificity-design heterodimer showed, most of the predicted side-chain packing interactions and a main-chain, conformation indistinguishable from the wild-type structure. These results, indicate that the design simulations capture important features of both, stability and structure and demonstrate that negative design can be, critical for attaining specificity when competing states are close in, structure space.
About this Structure
1ZSZ is a Protein complex structure of sequences from Haemophilus influenzae with MG as ligand. Full crystallographic information is available from OCA.
Reference
Specificity versus stability in computational protein design., Bolon DN, Grant RA, Baker TA, Sauer RT, Proc Natl Acad Sci U S A. 2005 Sep 6;102(36):12724-9. Epub 2005 Aug 29. PMID:16129838
Page seeded by OCA on Wed Nov 21 07:38:28 2007
Categories: Haemophilus influenzae | Protein complex | Baker, T.A. | Bolon, D.N. | Grant, R.A. | Sauer, R.T. | MG | Aaa | Adaptor | Protein design | Specificity
