Structural conservation of a short, functional, peptide-sequence motif

Document Type

Article

Publication Date

1-1-2009

Publication Title

Frontiers in Bioscience (Landmark Edition)

Volume

14

First page number:

1143

Last page number:

1151

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.

Keywords

Amino acid sequence; Bioinformatics; Computational biology; Conserved Sequence; Models; Molecular; Peptides/chemistry; Proteins—Conformation; Protein Conformation; Protein Domains; Proteins—Structure; Protein Structure; Review

Disciplines

Bioinformatics | Biology | Life Sciences | Molecular Biology | Structural Biology

Language

English

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