1tgg

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Revision as of 00:02, 25 November 2007

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spinqualitylabelsall models 1tgg, resolution 2.0Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

RH3 DESIGNED RIGHT-HANDED COILED COIL TRIMER

Overview

Designing new protein folds requires a method for simultaneously, optimizing the conformation of the backbone and the side-chains. One, approach to this problem is the use of a parameterized backbone, which, allows the systematic exploration of families of structures. We report the, crystal structure of RH3, a right-handed, three-helix coiled coil that was, designed using a parameterized backbone and detailed modeling of core, packing. This crystal structure was determined using another rationally, designed feature, a metal-binding site that permitted experimental phasing, of the X-ray data. RH3 adopted the intended fold, which has not been, observed previously in biological proteins. Unanticipated structural, asymmetry in the trimer was a principal source of variation within the RH3, structure. The sequence of RH3 differs from that of a previously, characterized right-handed tetramer, RH4, at only one position in each 11, amino acid sequence repeat. This close similarity indicates that the, design method is sensitive to the core packing interactions that specify, the protein structure. Comparison of the structures of RH3 and RH4, indicates that both steric overlap and cavity formation provide strong, driving forces for oligomer specificity.

About this Structure

1TGG is a Protein complex structure of sequences from [1] with NI, CL and ACE as ligands. Full crystallographic information is available from OCA.

Reference

Structural test of the parameterized-backbone method for protein design., Plecs JJ, Harbury PB, Kim PS, Alber T, J Mol Biol. 2004 Sep 3;342(1):289-97. PMID:15313624

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