The crystal structure of human receptor protein tyrosine phosphatase kappa phosphatase domain 1.
|Abstract||The receptor-type protein tyrosine phosphatases (RPTPs) are integral membrane proteins composed of extracellular adhesion molecule-like domains, a single transmembrane domain, and a cytoplasmic domain. The cytoplasmic domain consists of tandem PTP domains, of which the D1 domain is enzymatically active. RPTPkappa is a member of the R2A/IIb subfamily of RPTPs along with RPTPmu, RPTPrho, and RPTPlambda. Here, we have determined the crystal structur ... [truncated at 450 characters in length]|
|Author||Eswaran, Jeyanthy; Debreczeni, Judit E; Longman, Emma; et al|
|Subject||Amino Acid Sequence Binding Sites Crystallography, X-Ray Humans Models, Molecular Molecular Sequence Data Protein Conformation Protein Structure, Tertiary Protein Tyrosine Phosphatases Receptor-Like Protein Tyrosine Phosphatases, Class 2 Sequence Homology, Amino Acid Solutions Structural Homology, Protein chemistry metabolism|
Crystal structure of human protein tyrosine phosphatase 14 (PTPN14) at 1.65-A resolution.
|Author||Barr, Alastair J; Debreczeni, Judit E; Eswaran, Jeyanthy; et al|
|Subject||Amino Acid Sequence Binding Sites Crystallography, X-Ray Humans Models, Molecular Molecular Sequence Data Mutation Protein Structure, Tertiary Protein Tyrosine Phosphatase, Non-Receptor Type 1 Protein Tyrosine Phosphatases Protein Tyrosine Phosphatases, Non-Receptor Sequence Alignment Structural Homology, Protein genetics chemistry genetics metabolism|
MAPK-specific tyrosine phosphatases: new targets for drug discovery?
|Abstract||Protein tyrosine phosphatases (PTPs) have key roles in a diverse range of cellular processes, and their dysregulation is associated with several human diseases. Many PTPs are recognized as potential drug targets; however, inhibitor development has focused only on a small number of enzymes, most notably PTP1B for type II diabetes and obesity, and MKP1 and CDC25 for cancer. The future challenge of selective-inhibitor development for PTPs will be si ... [truncated at 450 characters in length]|
|Author||Barr, Alastair J; Knapp, Stefan;|
|Subject||Animals Crystallography, X-Ray Drug Design Humans Mitogen-Activated Protein Kinase Kinases Models, Molecular Phosphorylation Protein Tyrosine Phosphatases chemistry metabolism physiology chemistry metabolism physiology|
Large-scale structural analysis of the classical human protein tyrosine phosphatome.
|Abstract||Protein tyrosine phosphatases (PTPs) play a critical role in regulating cellular functions by selectively dephosphorylating their substrates. Here we present 22 human PTP crystal structures that, together with prior structural knowledge, enable a comprehensive analysis of the classical PTP family. Despite their largely conserved fold, surface properties of PTPs are strikingly diverse. A potential secondary substrate-binding pocket is frequently f ... [truncated at 450 characters in length]|
|Author||Barr, Alastair J; Ugochukwu, Emilie; Lee, Wen Hwa; et al|
|Subject||Amino Acid Sequence Crystallography, X-Ray Dimerization Humans Models, Molecular Protein Structure, Tertiary Protein Tyrosine Phosphatases Sequence Alignment Structure-Activity Relationship chemistry genetics metabolism|