Structural and evolutionary relationships among protein tyrosine phosphatase domains

Andersen, J. N., Mortensen, O. H., Peters, G. H., Drake, P. G., Iversen, L. F., Olsen, O. H., Jansen, P. G., Andersen, H. S., Tonks, N. K., Moller, N. P. H. (November 2001) Structural and evolutionary relationships among protein tyrosine phosphatase domains. Molecular and Cellular Biology, 21 (21). pp. 7117-7136. ISSN 0270-7306

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URL: http://www.ncbi.nlm.nih.gov/pubmed/11585896
DOI: 10.1128/mcb.21.21.7117-7136.2001

Abstract

With the current access to the whole genomes of various organisms and the completion of the first draft of the human genome, there is a strong need for a structure-function classification of protein families as an initial step in moving from DNA databases to a comprehensive understanding of human biology. As a result of the explosion in nucleic acid sequence information and the concurrent development of methods for high-throughput functional characterization of gene products, the genomic revolution also promises to provide a new paradigm for drug discovery, enabling the identification of molecular drug targets in a significant number of human diseases. This molecular view of diseases has contributed to the importance of combining primary sequence data with three-dimensional structure and has increased the awareness of computational homology modeling and its potential to elucidate protein function. In particular, when important proteins or novel therapeutic targets are identified—like the family of protein tyrosine phosphatases (PTPs) (reviewed in reference 53)—a structure-function classification of such protein families becomes an invaluable framework for further advances in biomedical science. Here, we present a comparative analysis of the structural relationships among vertebrate PTP domains and provide a comprehensive resource for sequence analysis of phosphotyrosine-specific PTPs.

Item Type: Paper
Uncontrolled Keywords: SUBSTRATE-TRAPPING MUTANTS MOLECULAR-DYNAMICS SIMULATIONS TANDEM CATALYTIC DOMAINS MEMBRANE-DISTAL DOMAIN 2 POINT MUTATIONS CRYSTAL-STRUCTURE INSULIN SENSITIVITY CYTOPLASMIC DOMAIN TRANSITION-STATE SIGNATURE MOTIF
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification
evolution
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > protein tyrosine phosphatase
CSHL Authors:
Communities: CSHL labs > Tonks lab
Depositing User: Matt Covey
Date: November 2001
Date Deposited: 18 Dec 2013 19:47
Last Modified: 18 Dec 2013 19:47
PMCID: PMC99888
Related URLs:
URI: http://repository.cshl.edu/id/eprint/29020

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