Identification of specific lipid-binding sites in integral membrane proteins

Autor: Marc F. Lensink, Cédric Govaerts, Jean Marie Ruysschaert
Rok vydání: 2010
Předmět:
Models
Molecular

Membrane Fluidity
Protein Conformation
Biochimie
Lipid Bilayers
Phosphatidylcholines -- metabolism
Sciences de la matière vivante
Biophysique
Molecular Dynamics Simulation
Biochemistry
Lipid Bilayers -- metabolism
Orientations of Proteins in Membranes database
Lipid Bilayers -- chemistry
Phosphatidylcholines -- chemistry
Membrane Proteins -- metabolism
Protein–lipid interaction
Molecular Biology
Integral membrane protein
Binding Sites
Chemistry
Peripheral membrane protein
Biologie moléculaire
Membrane Proteins
Membrane Transport Proteins
Computational Biology
Biological membrane
Hydrogen Bonding
Cell Biology
Sciences bio-médicales et agricoles
Membrane transport
Sciences biomédicales
Membrane Transport Proteins -- chemistry
Membrane protein
Membrane Proteins -- chemistry
Phosphatidylcholines
Biologie cellulaire
Membrane Transport Proteins -- metabolism
lipids (amino acids
peptides
and proteins)

Biologie
Membrane biophysics
Zdroj: The Journal of biological chemistry, 285 (14
ISSN: 1083-351X
Popis: Protein-lipid interactions are increasingly recognized as central to the structure and function of membrane proteins. However, with the exception of simplified models, specific protein-lipid interactions are particularly difficult to highlight experimentally. Here, we used molecular dynamics simulations to identify a specific protein-lipid interaction in lactose permease, a prototypical model for transmembrane proteins. The interactions can be correlated with the functional dependence of the protein to specific lipid species. The technique is simple and widely applicable to other membrane proteins, and a variety of lipid matrices can be used.
Journal Article
Research Support, Non-U.S. Gov't
SCOPUS: ar.j
info:eu-repo/semantics/published
Databáze: OpenAIRE