Investigating the conformational coupling between the transmembrane and cytoplasmic domains of a single-spanning membrane protein. A 1H-NMR study.
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.
Mousson
F
F
Biophysique des Protéines et des Membranes, CEA DSV/DBCM and URA CNRS 2096, Centre d'Etudes de Saclay, Gif sur Yvette, France.
Beswick
V
V
Coïc
Y M
YM
Huynh-Dinh
T
T
Sanson
A
A
Neumann
J M
JM
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
D008565:Membrane Proteins; D008823:Micelles; D011510:Proteolipids; D011522:Protons