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|
HD-PTP is a catalytically inactive tyrosine phosphatase due to a conserved divergence in its phosphatase domain.
|Abstract||The HD-PTP protein has been described as a tumor suppressor candidate and based on its amino acid sequence, categorized as a classical non-transmembrane protein tyrosine phosphatase (PTP). To date, no HD-PTP phosphorylated substrate has been identified and controversial results concerning its catalytic activity have been recently reported.|
|Author||Gingras, Marie-Claude; Zhang, Yu Ling; Kharitidi, Dmitri; et al|
|Subject||Amino Acid Sequence Catalysis Cell Line Conserved Sequence DNA, Complementary Humans Kinetics Protein Tyrosine Phosphatases, Non-Receptor Sequence Homology, Amino Acid chemistry genetics metabolism|