Toll-like receptor 3 transmembrane domain is able to perform various homotypic interactions: An NMR structural study

FEBS Letters

Volumn 588, Issue 21, 2014, Pages 3802-3807

  Mineev, Konstantin S ^a   Goncharuk, Sergey A ^a,b   Arseniev, Alexander S ^a  

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

^b MOSCOW STATE UNIVERSITY   (Russian Federation)

Author keywords

Dimerization; Free energy; Spatial structure; Toll like receptor; Transmembrane domain

Indexed keywords

DETERGENT; DIMER; DODECYLPHOSPHORYLCHOLINE; POLYMER; TOLL LIKE RECEPTOR 3; TRIMER; UNCLASSIFIED DRUG; MICELLE; PHOSPHORYLCHOLINE; PROTEIN BINDING; TLR3 PROTEIN, HUMAN;

ARTICLE; ENERGY EXPENDITURE; MICELLE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN DOMAIN; PROTEIN INTERACTION; PROTEIN MODIFICATION; PROTEIN PURIFICATION; PROTEIN STRUCTURE; SIGNAL TRANSDUCTION; SOLUBILIZATION; AMINO ACID SEQUENCE; ANALOGS AND DERIVATIVES; CELL MEMBRANE; CHEMICAL STRUCTURE; CHEMISTRY; HUMAN; METABOLISM; MOLECULAR GENETICS; PROTEIN MULTIMERIZATION; PROTEIN QUATERNARY STRUCTURE; PROTEIN STABILITY; PROTEIN TERTIARY STRUCTURE; THERMODYNAMICS;

AMINO ACID SEQUENCE; CELL MEMBRANE; HUMANS; MAGNETIC RESONANCE SPECTROSCOPY; MICELLES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PHOSPHORYLCHOLINE; PROTEIN BINDING; PROTEIN MULTIMERIZATION; PROTEIN STABILITY; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; THERMODYNAMICS; TOLL-LIKE RECEPTOR 3;

EID: 84908318473     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2014.08.031     Document Type: Article

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