title: Prostaglandin H synthase: implications for membrane structure.
abstract: The crystal structure of the membrane protein prostaglandin H synthase (PGHS) provides strong evidence for the existence of monotopic membrane proteins: PGHS seems to interact with the membrane via a motif of amphipathic helices positioned parallel to the plane of the membrane. The orientation of this unique membrane binding motif is fixed in space by an epidermal growth factor(EGF)-like module on its amino-terminal end and by the catalytic domain at its carboxy-terminal end. The catalytic domain of PGHS has a high structural homology to other mammalian heme peroxidases.
authors.affiliation: Department of Biochemistry and Molecular Biology, University of Chicago, IL 60637.
authors.forename: D
authors.initials: D
authors.lastname: Picot
authors.forename: R M
authors.initials: RM
authors.lastname: Garavito
mesh_terms: D000595:Amino Acid Sequence; D003460:Crystallization; D046911:Macromolecular Substances; D008565:Membrane Proteins / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011451:Prostaglandin-Endoperoxide Synthases / Q000737:chemistry*; D017433:Protein Structure, Secondary
chemical_list: D046911:Macromolecular Substances; D008565:Membrane Proteins; D011451:Prostaglandin-Endoperoxide Synthases