Abstract
In the past few years, very rapid advances have been made in determining the primary structure of protein tyrosine phosphatases (PTPases). PTPase genes have now been isolated from bacteria, viruses, yeasts and insects as well as vertebrates. The cytosolic PTPases have a catalytic domain associated with various accessory domains that are believed to be involved in protein-protein interaction or subcellular localization. The transmembrane PTPases have either one or two cytoplasmic PTPase domains and an extracellular receptor-like structure. The existence of a large number of structurally diverse PTPases suggests that they play specific and crucial roles in signal transduction. In this article, the structural features of the PTPases from higher eukaryotes are reviewed.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
