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1qys
From Proteopedia
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Crystal structure of Top7: A computationally designed protein with a novel fold
Overview
A major challenge of computational protein design is the creation of novel proteins with arbitrarily chosen three-dimensional structures. Here, we used a general computational strategy that iterates between sequence design and structure prediction to design a 93-residue alpha/beta protein called Top7 with a novel sequence and topology. Top7 was found experimentally to be folded and extremely stable, and the x-ray crystal structure of Top7 is similar (root mean square deviation equals 1.2 angstroms) to the design model. The ability to design a new protein fold makes possible the exploration of the large regions of the protein universe not yet observed in nature.
About this Structure
1QYS is a Protein complex structure of sequences from Computationally designed sequence. The following page contains interesting information on the relation of 1QYS with [Designer Proteins]. Full crystallographic information is available from OCA.
Reference
Design of a novel globular protein fold with atomic-level accuracy., Kuhlman B, Dantas G, Ireton GC, Varani G, Stoddard BL, Baker D, Science. 2003 Nov 21;302(5649):1364-8. PMID:14631033
Page seeded by OCA on Thu Mar 20 13:44:31 2008
