Ligand binding pocket formed by evolutionarily conserved residues in the glucagon-like peptide-1 (GLP-1) receptor core domain

Journal of Biological Chemistry

Volumn 290, Issue 9, 2015, Pages 5696-5706

  Moon, Mi Jin ^a   Lee, Yoo Na ^a   Park, Sumi ^a   Reyes Alcaraz, Arfaxad ^a   Hwang, Jong Ik ^a   Millar, Robert Peter ^b,d   Choe, Han ^c   Seong, Jae Young ^a  

^a Korea University College of Medicine   (South Korea)

^b UNIVERSITY OF PRETORIA   (South Africa)

^c University of Ulsan College of Medicine   (South Korea)

^d UNIVERSITY OF EDINBURGH   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; MOLECULAR INTERACTIONS; PEPTIDES;

AMINO ACID RESIDUES; GLUCAGON-LIKE PEPTIDE-1; GLUCOSE HOMEOSTASIS; HIGH-AFFINITY LIGAND BINDING; MOLECULAR MECHANISM; MOLECULAR MODELING STUDIES; RECEPTOR ACTIVATION; TRANSMEMBRANE HELICES;

LIGANDS;

ARGININE; ASPARTIC ACID; GLUCAGON LIKE PEPTIDE 1 RECEPTOR; GLYCINE; HISTIDINE; ISOLEUCINE; LEUCINE; PHENYLALANINE; THREONINE; AMINO ACID; GLP1R PROTEIN, HUMAN; GLUCAGON LIKE PEPTIDE 1; GLUCAGON RECEPTOR; LIGAND; PEPTIDE; PROTEIN BINDING;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; BINDING AFFINITY; BINDING SITE; CHIMERA; CONTROLLED STUDY; EXTRACELLULAR SPACE; GENETIC CONSERVATION; HUMAN; HUMAN CELL; HYDROPHOBICITY; LIGAND BINDING; MOLECULAR EVOLUTION; MOLECULAR INTERACTION; MOLECULAR MODEL; POINT MUTATION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DOMAIN; RECEPTOR UPREGULATION; CHEMICAL STRUCTURE; CHEMISTRY; CONSERVED SEQUENCE; GENETICS; HEK293 CELL LINE; METABOLISM; MOLECULAR GENETICS; PROTEIN TERTIARY STRUCTURE; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; AMINO ACIDS; BINDING SITES; CONSERVED SEQUENCE; EVOLUTION, MOLECULAR; GLUCAGON-LIKE PEPTIDE 1; GLUCAGON-LIKE PEPTIDE-1 RECEPTOR; HEK293 CELLS; HUMANS; LIGANDS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PEPTIDES; POINT MUTATION; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; RECEPTORS, GLUCAGON; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 84923767681     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.612606     Document Type: Article

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