Alternative packing of EGFR transmembrane domain suggests that protein-lipid interactions underlie signal conduction across membrane

Biochimica et Biophysica Acta - Biomembranes

Volumn 1858, Issue 6, 2016, Pages 1254-1261

  Bocharov, Eduard V ^a   Lesovoy, Dmitry M ^a   Pavlov, Konstantin V ^a   Pustovalova, Yulia E ^a   Bocharova, Olga V ^a   Arseniev, Alexander S ^a  

^a SHEMYAKIN OVCHINNIKOV INSTITUTE OF BIOORGANIC CHEMISTRY   (Russian Federation)

Author keywords

Dimerization; NMR; Protein lipid interactions; Receptor tyrosine kinase; Spatial structure; Transmembrane domain

Indexed keywords

EPIDERMAL GROWTH FACTOR RECEPTOR; PHOSPHOTRANSFERASE; MEMBRANE LIPID; MEMBRANE PROTEIN;

ALPHA HELIX; AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ENZYME INHIBITION; HUMAN; HYDROGEN BOND; HYDROPHOBICITY; LIGAND BINDING; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN LIPID INTERACTION; PROTEIN MOTIF; PROTEIN PROTEIN INTERACTION; RECEPTOR BINDING; SIGNAL TRANSDUCTION; AMINO ACID SEQUENCE; CELL MEMBRANE; CHEMISTRY; DIMERIZATION; METABOLISM; MOLECULAR GENETICS; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; CELL MEMBRANE; DIMERIZATION; MEMBRANE LIPIDS; MEMBRANE PROTEINS; MOLECULAR SEQUENCE DATA; RECEPTOR, EPIDERMAL GROWTH FACTOR; SEQUENCE HOMOLOGY, AMINO ACID; SIGNAL TRANSDUCTION;

EID: 84962568117     PISSN: 00052736     EISSN: 18792642     Source Type: Journal    
DOI: 10.1016/j.bbamem.2016.02.023     Document Type: Article

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