Sequences annotated by structure: a tool to facilitate the use of structural information in sequence analysis

With the aim of bridging the gap between protein sequence and structural analyses, we have developed a tool to aid the identification of new protein sequences by recognizing distant homologues using structural information. The tool generates sequence annotated by structure (SAS) files, applying stru...

Full description

Saved in:
Bibliographic Details
Published in:Protein engineering 1998-10, Vol.11 (10), p.855-859
Main Authors: Milburn, D, Laskowski, R A, Thornton, J M
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Binding Sites
Databases, Factual
DNA-Binding Proteins - chemistry
Hydrogen Bonding
Internet
Lactalbumin - chemistry
Lactalbumin - metabolism
Ligands
Metals - metabolism
Molecular Sequence Data
Muramidase - chemistry
Muramidase - metabolism
Protein Conformation
Protein Folding
Protein Structure, Secondary
Proteins - chemistry
Sequence Alignment
Sequence Analysis
Sequence Homology, Amino Acid
Software
Structure-Activity Relationship
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:With the aim of bridging the gap between protein sequence and structural analyses, we have developed a tool to aid the identification of new protein sequences by recognizing distant homologues using structural information. The tool generates sequence annotated by structure (SAS) files, applying structural information derived from structural analyses to a given protein sequence. A World Wide Web interface allows a given sequence to be submitted either for structural annotation or, where its structure is unknown, for search and alignment against sequences of known structure. In both cases, SAS will colour residues in the sequence of known structure according to a selection of properties, including secondary structure, interatomic contacts and active site information. SAS can also be used to inspect properties of a single structure.
ISSN:0269-2139
1741-0126
1741-0134
DOI:10.1093/protein/11.10.855