Motivated proteins: a web application for studying small three-dimensional protein motifs

Leader, D.P., and Milner-White, E.J. (2009) Motivated proteins: a web application for studying small three-dimensional protein motifs. BMC Bioinformatics, 10(60), (doi:10.1186/1471-2105-10-60)

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Publisher's URL: http://dx.doi.org/10.1186/1471-2105-10-60

Abstract

BACKGROUND: Small loop-shaped motifs are common constituents of the three-dimensional structure of proteins. Typically they comprise between three and seven amino acid residues, and are defined by a combination of dihedral angles and hydrogen bonding partners. The most abundant of these are alphabeta-motifs, asx-motifs, asx-turns, beta-bulges, beta-bulge loops, beta-turns, nests, niches, Schellmann loops, ST-motifs, ST-staples and ST-turns.We have constructed a database of such motifs from a range of high-quality protein structures and built a web application as a visual interface to this. DESCRIPTION: The web application, Motivated Proteins, provides access to these 12 motifs (with 48 sub-categories) in a database of over 400 representative proteins. Queries can be made for specific categories or sub-categories of motif, motifs in the vicinity of ligands, motifs which include part of an enzyme active site, overlapping motifs, or motifs which include a particular amino acid sequence. Individual proteins can be specified, or, where appropriate, motifs for all proteins listed. The results of queries are presented in textual form as an (X)HTML table, and may be saved as parsable plain text or XML. Motifs can be viewed and manipulated either individually or in the context of the protein in the Jmol applet structural viewer. Cartoons of the motifs imposed on a linear representation of protein secondary structure are also provided. Summary information for the motifs is available, as are histograms of amino acid distribution, and graphs of dihedral angles at individual positions in the motifs. CONCLUSION: Motivated Proteins is a publicly and freely accessible web application that enables protein scientists to study small three-dimensional motifs without requiring knowledge of either Structured Query Language or the underlying database schema

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Milner-White, Professor E and Leader, Dr David
Authors: Leader, D.P., and Milner-White, E.J.
Subjects:Q Science > QR Microbiology
College/School:College of Medical Veterinary and Life Sciences
Journal Name:BMC Bioinformatics
ISSN:1471-2105
Copyright Holders:Copyright © 2009 BMC
First Published:First published in BMC Bioinformatics 10(60)
Publisher Policy:Reproduced in accordance with the copyright policy of the publisher

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