title: Production and crystallization of a panel of structure-based mutants of the human myelin peripheral membrane protein P2.
abstract: The myelin sheath is a multilayered membrane that surrounds and insulates axons in the nervous system. One of the proteins specific to the peripheral nerve myelin is P2, a protein that is able to stack lipid bilayers. With the goal of obtaining detailed information on the structure-function relationship of P2, 14 structure-based mutated variants of human P2 were generated and produced. The mutants were designed to potentially affect the binding of lipid bilayers by P2. All mutated variants were also crystallized and preliminary crystallographic data are presented. The structural data from the mutants will be combined with diverse functional assays in order to elucidate the fine details of P2 function at the molecular level.
authors.affiliation: Department of Biochemistry and Biocenter Oulu, Universtity of Oulu, PO Box 3000, 90014 Oulu, Finland.
authors.forename: Mari
authors.initials: M
authors.lastname: Lehtimäki
authors.forename: Saara
authors.initials: S
authors.lastname: Laulumaa
authors.forename: Salla
authors.initials: S
authors.lastname: Ruskamo
authors.forename: Petri
authors.initials: P
authors.lastname: Kursula
mesh_terms: D019943:Amino Acid Substitution; D003460:Crystallization; D004926:Escherichia coli; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D008958:Models, Molecular; D016297:Mutagenesis, Site-Directed; D018996:Myelin P2 Protein / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics*; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D014961:X-Ray Diffraction
chemical_list: D018996:Myelin P2 Protein