Targeting of proteins for structure determination in structural genomic programs often includes the use of threading and fold recognition methods to exclude proteins belonging to well-populated fold families, but such methods can still fail to recognize preexisting folds. The authors illustrate here a method in which limited amounts of structural data are used to improve an initial homology search and the data are subsequently used to produce a structure by data-constrained refinement of an identified structural template. The data used are primarily NMR-based residual dipolar couplings, but they also include additional chemical shift and backbone-nuclear Overhauser effect data. Using this methodology, a backbone structure was efficiently produced for a 10 kDa protein (PF1455) from Pyrococcus furiosus. Its relationship to existing structures and its probable function are discussed. © 2006 Wiley-Liss, Inc.
Available at: http://works.bepress.com/francis_jenney/26/
This article was published in Proteins: Structure, Function and Genetics, Volume 65, Issue 2, Pages 480-489.
The published version is available at http://dx.doi.org/10.1002/prot.21119.Copyright © 2006 Wiley.