SnapDRAGON: a method to delineate protein structural domains from sequence data

JOURNAL OF MOLECULAR BIOLOGY

卷:316

Article

George, RA ; Heringa, J

关键词: protein;    domain;    boundaries;    prediction;    folding;   

DOI  :  10.1006/jmbi.2001.5387

来源: Elsevier

【 摘 要 】

We describe a method to identify protein domain boundaries from sequence information alone based on the assumption that hydrophobic residues cluster together in space. SnapDRAGON is a suite of programs developed to predict domain boundaries based on the consistency observed in a set of alternative ab initio three-dimensional (3D) models generated for a given protein multiple sequence alignment. This is achieved by running a distance geometry-based folding technique in conjunction with a 3D-domain assignment algorithm. The overall accuracy of our method in predicting the number of domains for a non-redundant data set of 414 multiple alignments, representing 185 single and 231 multiple-domain proteins, is 72.4%. Using domain linker regions observed in the tertiary structures associated with each query alignment as the standard of truth, inter-domain boundary positions are delineated with an accuracy of 63.9% for proteins comprising continuous domains only, and 35.4% for proteins with discontinuous domains. Overall, domain boundaries are delineated with an accuracy of 51.8%. The prediction accuracy values are independent of the pair-wise sequence similarities within each of the alignments. These results demonstrate the capability of our method to delineate domains in protein sequences associated with a wide variety of structural domain organisation. (C) 2002 Elsevier Science Ltd.

【 授权许可】

Free