title: Investigating the conformational coupling between the transmembrane and cytoplasmic domains of a single-spanning membrane protein. A 1H-NMR study.
abstract: PMP1 is a 38-residue single-spanning membrane protein whose C-terminal cytoplasmic domain, Y25-F38, is highly positively charged. The conformational coupling between the transmembrane span and the cytoplasmic domain of PMP1 was investigated from 1H-nuclear magnetic resonance data of two synthetic fragments: F9-F38, i.e. 80% of the whole sequence, and Y25-F38, the isolated cytoplasmic domain. Highly disordered in aqueous solution, the Y25-F38 peptide adopts a well-defined conformation in the presence of dodecylphosphocholine micelles. Compared with the long PMP1 fragment, this structure exhibits both native and non-native elements. Our results make it possible to assess the influence of a hydrophobic anchor on the intrinsic conformational propensity of a cytoplasmic domain.
authors.affiliation: Biophysique des Protéines et des Membranes, CEA DSV/DBCM and URA CNRS 2096, Centre d'Etudes de Saclay, Gif sur Yvette, France.
authors.forename: F
authors.initials: F
authors.lastname: Mousson
authors.forename: V
authors.initials: V
authors.lastname: Beswick
authors.forename: Y M
authors.initials: YM
authors.lastname: Coïc
authors.forename: T
authors.initials: T
authors.lastname: Huynh-Dinh
authors.forename: A
authors.initials: A
authors.lastname: Sanson
authors.forename: J M
authors.initials: JM
authors.lastname: Neumann
mesh_terms: D000595:Amino Acid Sequence; D002462:Cell Membrane / Q000378:metabolism; D003593:Cytoplasm / Q000378:metabolism; D008565:Membrane Proteins / Q000737:chemistry* / Q000378:metabolism; D008823:Micelles; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation; D011510:Proteolipids / Q000737:chemistry* / Q000378:metabolism; D011522:Protons
chemical_list: D008565:Membrane Proteins; D008823:Micelles; D011510:Proteolipids; D011522:Protons