title: Successful ab initio prediction of the tertiary structure of NK-lysin using multiple sequences and recognized supersecondary structural motifs.
abstract: A simple approach to protein tertiary structure prediction is described, based on the assembly of recognized supersecondary structural fragments taken from highly resolved protein structures by using a simulated annealing algorithm. The results of blind-testing this method on CASP2 target T0042 (pig NK-lysin) are presented. The predicted structure had a C alpha root-mean-square deviation of only 6.2 A from the experimental structure (and less than 5.0 A over the first 66 residues), and clearly had the correct fold when judged by using a number of objective measures. Despite the significant degree of success in this case, there is clearly much more development required before predictions with the accuracy of a good homology model can be made with this kind of approach.
authors.affiliation: Department of Biological Sciences, University of Warwick, Coventry, United Kingdom.
authors.forename: D T
authors.initials: DT
authors.lastname: Jones
mesh_terms: D000890:Anti-Infective Agents / Q000737:chemistry*; D000970:Antineoplastic Agents / Q000737:chemistry*; D001665:Binding Sites; D008958:Models, Molecular; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011510:Proteolipids / Q000737:chemistry*; D011663:Pulmonary Surfactants / Q000737:chemistry*
chemical_list: D000890:Anti-Infective Agents; D000970:Antineoplastic Agents; C093238:NK-lysin; D011510:Proteolipids; D011663:Pulmonary Surfactants