Open Access
Article
Structural conservation of a short, functional, peptide-sequence motif
Susan Fox-Erlich1,Martin R Schiller1,Michael R Gryk1
1
Department of Molecular, Microbial and Structural Biology, University of Connecticut Health Center, 263 Farmington Avenue, Farmington, CT 06030-3305, USA
DOI: 10.2741/3299 Volume 14 Issue 3, pp.1143-1151
Published: 01 January 2009
(This article belongs to the Special Issue Short function motifs in proteins)
Abstract

Full length, eukaryotic proteins generally consist of several autonomously folding and functioning domains. Many of these domains are known to function by binding and/or modifying other partner proteins based on the recognition of a short, linear amino sequence contained within the target protein. This article reviews the many bioinformatic tools and resources which discover, define and catalogue the various, known protein domains as well as assist users by identifying domain signatures within proteins of interest. We also review the smaller subset of bioinformatic tools which catalogue and help identify the short linear motifs used for domain targeting. It has been suggested that these short, functional, peptide-sequence motifs are normally found in unstructured regions of the target. The role of protein structure in the activity of one representative of these short, functional motifs is explored through an examination of known structures deposited in the Protein Data Bank.

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Susan Fox-Erlich, Martin R Schiller, Michael R Gryk. Structural conservation of a short, functional, peptide-sequence motif. Frontiers in Bioscience-Landmark. 2009. 14(3); 1143-1151.