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|