title: Structure and regulation of the c-Fes protein-tyrosine kinase.
abstract: The c-Fes protein-tyrosine kinase is the normal cellular ortholog of several avian and feline retroviral oncoproteins. Unlike its transforming viral counterparts, c-Fes tyrosine kinase activity is tightly regulated in vivo through a mechanism involving coiled-coil oligomerization domains and other unique structural features found in its long N-terminal region. This review is focused on the regulatory features and structural biology of c-Fes, which has been implicated in normal cellular growth regulation, the innate immune response, and tumorigenesis.
authors.affiliation: Department of Microbiology and Molecular Genetics, University of Pittsburgh School of Medicine, Pittsburgh, PA 15219, USA.
authors.forename: Sabine
authors.initials: S
authors.lastname: Hellwig
authors.forename: Thomas E
authors.initials: TE
authors.lastname: Smithgall
mesh_terms: D000818:Animals; D000906:Antibodies; D001854:Bone Marrow Cells / Q000201:enzymology; D002471:Cell Transformation, Neoplastic; D002472:Cell Transformation, Viral; D015681:Fusion Proteins, gag-onc / Q000276:immunology; D006801:Humans; D009857:Oncogenes; D017434:Protein Structure, Tertiary; D051578:Proto-Oncogene Proteins c-fes / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*
chemical_list: D000906:Antibodies; D015681:Fusion Proteins, gag-onc; D051578:Proto-Oncogene Proteins c-fes