Langerin-heparin interaction: Two binding sites for small and large ligands as revealed by a combination of NMR spectroscopy and cross-linking mapping experiments

Journal of the American Chemical Society

Volumn 137, Issue 12, 2015, Pages 4100-4110

  Muñoz García, Juan C ^a,f   Chabrol, Eric ^b,c   Vivès, Romain R ^b,c   Thomas, Aline ^d   De Paz, José L ^a   Rojo, Javier ^a   Imberty, Anne ^d   Fieschi, Franck ^b,c   Nieto, Pedro M ^a   Angulo, Jesús ^a,e  

^a INSTITUTO DE INVESTIGACIONES QUÍMICAS   (Spain)

^b INSTITUT DE BIOLOGIE STRUCTURALE   (France)

^c CEA GRENOBLE   (France)

^d UNIV GRENOBLE ALPES   (France)

^e UNIVERSITY OF EAST ANGLIA   (United Kingdom)

^f UNIVERSITY OF OXFORD   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; CALCIUM; CARBOHYDRATES; CARBOXYLATION; EPITOPES; LIGANDS; MOBILE SECURITY; MOLECULAR DYNAMICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; POLYSACCHARIDES; PROTEINS;

CARBOHYDRATE LIGANDS; CELLULAR ORGANELLES; EQUATORIAL HYDROXYL GROUPS; EXTRACELLULAR DOMAINS; PARTICLE TRANSMISSION; SATURATION TRANSFER DIFFERENCE NMR; SUBSTITUTION PATTERNS; SULFATED GLYCOSAMINOGLYCANS;

BINDING SITES;

CALCIUM; CARBOXYLIC ACID; GLYCOSAMINOGLYCAN POLYSULFATE; HEPARIN; HYDROXYL GROUP; IDURONIC ACID; LANGERIN; LIGAND; CD207 PROTEIN, HUMAN; DIVALENT CATION; LECTIN; LEUKOCYTE ANTIGEN; MANNOSE BINDING LECTIN; OLIGOSACCHARIDE; TRISACCHARIDE;

ARTICLE; CROSS LINKING; DRUG RECEPTOR BINDING; INFORMATION; LIGAND BINDING; MOLECULAR DOCKING; MOLECULAR DYNAMICS; MOLECULAR RECOGNITION; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; NUCLEAR OVERHAUSER EFFECT; AMINO ACID SEQUENCE; ANALOGS AND DERIVATIVES; BINDING SITE; CHEMISTRY; HUMAN; METABOLISM; MOLECULAR GENETICS; NUCLEAR MAGNETIC RESONANCE; PROCEDURES;

AMINO ACID SEQUENCE; ANTIGENS, CD; BINDING SITES; CALCIUM; CATIONS, DIVALENT; HEPARIN; HUMANS; LECTINS, C-TYPE; MANNOSE-BINDING LECTINS; MOLECULAR DOCKING SIMULATION; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; OLIGOSACCHARIDES; TRISACCHARIDES;

EID: 84926300956     PISSN: 00027863     EISSN: 15205126     Source Type: Journal    
DOI: 10.1021/ja511529x     Document Type: Article

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