2f40

Publication Abstract from PubMed

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.

Structure determination of a new protein from backbone-centered NMR data and NMR-assisted structure prediction.,Mayer KL, Qu Y, Bansal S, LeBlond PD, Jenney FE Jr, Brereton PS, Adams MW, Xu Y, Prestegard JH Proteins. 2006 Nov 1;65(2):480-9. PMID:16927360^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.