1qys
From Proteopedia
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
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 Sat May 3 06:51:58 2008
