Bioinformatics. 1998;14(7):617-23.

JOY: protein sequence-structure representation and analysis.

Mizuguchi K, Deane CM, Blundell TL, Johnson MS, Overington JP.

Source

Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1GA, UK. kenji@cryst.bioc.cam.ac.uk

Abstract

MOTIVATION:

JOY is a program to annotate protein sequence alignments with three-dimensional (3D) structural features. It was developed to display 3D structural information in a sequence alignment and to help understand the conservation of amino acids in their specific local environments.

RESULTS:

: The JOY representation now constitutes an essential part of the two databases of protein structure alignments: HOMSTRAD (http://www-cryst.bioc.cam.ac.uk/homstrad ) and CAMPASS (http://www-cryst.bioc.cam.ac. uk/campass). It has also been successfully used for identifying distant evolutionary relationships.

AVAILABILITY:

The program can be obtained via anonymous ftp from torsa.bioc.cam.ac.uk from the directory /pub/joy/. The address for the JOY server is http://www-cryst.bioc.cam.ac.uk/cgi-bin/joy.cgi.

CONTACT:

kenji@cryst.bioc.cam.ac.uk

PMID:: 9730927; [PubMed - indexed for MEDLINE]

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Publication Types, MeSH Terms, Substances

Publication Types

Research Support, Non-U.S. Gov't

MeSH Terms

Substances

Proteins

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JOY - Bioinformatics.ca Links Directory

Miscellaneous

BioSharing: biological databases: Structural motifs of protein superfamilies - Neuroscience Information Framework

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