Structural and Evolutionary Relationships among Protein Tyrosine Phosphatase Domains

By J. Andersen, O. Mortensen, G. Peters, P. Drake, L. Iversen, O. Olsen, P. Jansen, H. Andersen, N. Tonks, N. P. Møller. Molecular and Cellular Biology, 2001

713 citations recorded by the source corpus.

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.

Subfields: Immunology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/0b018aea2bc8cc8ba718d8777ce2913841fc5bdd

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Immunology

1. C. Hellberg
2. F. Böhmer
3. A. Ostman
4. M. Reth
5. N. Tonks

In Molecular Biology

1. C. Hellberg
2. F. Böhmer
3. A. Ostman
4. M. Reth
5. N. Tonks
6. J. Ferrell
7. Jeffrey A. Ubersax
8. Boris N. Kholodenko

Citations in the corpus

• Protein tyrosine phosphatases: from genes, to function, to disease (2006, background): “The catalytic domain of classical PTPs comprises approximately 280 residues and is defined by several short sequence motifs, in particular the signature sequence that functions as a phosphate-binding loop at the active sit”
• The role of JAK-STAT signaling pathway and its regulators in the fate of T helper cells (2017, background): “CD45 is a receptor which is highly expressed by hematopoietic cells, especially B and T cells [89].”
• Metabolic Syndrome and Insulin Resistance: Underlying Causes and Modification by Exercise Training (2013, neutral): “In general, PTPases are redox sensitive enzymes and all share a common catalytic motif (21).”
• Hydrogen peroxide as second messenger in lymphocyte activation (2002, background): “All PTPs contain, in their catalytic center, a reactive and redox-regulated cysteine in the vicinity of a positive charge with the sequence motif (HCxxGxxRS/T”
• Protein-tyrosine phosphatases and cancer (2006, background): “It is now known that PTPs constitute a large, structurally diverse family of tightly regulated, highly specific enzymes with important regulatory roles (for reviews see Refs”
• The Role of Selenium in Inflammation and Immunity: From Molecular Mechanisms to Therapeutic Opportunities (2012, background): “An example of this signaling mechanism that is particularly important for immune cells is the PTPs, which contain a redox-regulated Cys in the proper context (HCxxGxxRS/T) (7, 184).”
• Mechanisms of specificity in protein phosphorylation (2007, background): “Interestingly, this same feature contributes to the specificity of Tyr phosphatases and Ser/Thr phosphatase”