title: Structure and catalytic mechanism of human protein tyrosine phosphatome.
abstract: Together with protein tyrosine kinases (PTKs), protein tyrosine phosphatases (PTPs) serve as hallmarks in cellular signal transduction by controlling the reversible phosphorylation of their substrates. The human genome is estimated to encode more than 100 PTPs, which can be divided into eleven sub-groups according to their structural and functional characteristics. All the crystal structures of catalytic domains of sub-groups have been elucidated, enabling us to understand their precise catalytic mechanism and to compare their structures across all sub-groups. In this review, I describe the structure and mechanism of catalytic domains of PTPs in the structural context.
authors.affiliation: Medical Proteomics Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon 305-333, Korea. ksj@kribb.re.kr
authors.forename: Seung Jun
authors.initials: SJ
authors.lastname: Kim
authors.forename: Seong Eon
authors.initials: SE
authors.lastname: Ryu
mesh_terms: D055162:Biocatalysis; D020134:Catalytic Domain; D006801:Humans; D010766:Phosphorylation; D017027:Protein Tyrosine Phosphatases / Q000737:chemistry / Q000145:classification / Q000378:metabolism*
chemical_list: D017027:Protein Tyrosine Phosphatases