Functional differences of invariant and highly conserved residues in the extracellular domain of the glycoprotein hormone receptors

Journal of Biological Chemistry

Volumn 285, Issue 45, 2010, Pages 34813-34827

  Angelova, Krassimira ^a   De Jonge, Hugo ^b   Granneman, Joke C M ^b   Puett, David ^a   Bogerd, Jan ^b  

^a University of Georgia ^*  (United States)

^b UTRECHT UNIVERSITY   (Netherlands)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID RESIDUES; COMPARATIVE MODELING; COMPARATIVE STUDIES; CONSERVED RESIDUES; CONTACT SITES; EXTRACELLULAR DOMAINS; FOLLICLE STIMULATING HORMONE; FUNCTIONAL CHARACTERIZATION; GLYCOPROTEIN HORMONE RECEPTORS; GLYCOPROTEIN HORMONES; HORMONE BINDING; HORMONE RECEPTORS; HUMAN RECEPTORS; MULTIPLE INTERACTIONS; N-TERMINALS; NON-CONTACT; RECEPTOR ACTIVATION; RECEPTOR INTERACTION; STRUCTURAL INFORMATION;

ACTIVATION ANALYSIS; AMINO ACIDS; BINDING SITES; COMPLEXATION; ENDOCRINOLOGY; FETAL MONITORING; GLYCOPROTEINS; HORMONES; REDUCTION;

CRYSTAL STRUCTURE;

ASPARAGINE; ASPARTIC ACID; CYCLIC AMP; GLYCOPROTEIN HORMONE RECEPTOR; HORMONE RECEPTOR; LYSINE; RECEPTOR PROTEIN; SERINE; THREONINE; TYROSINE; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; BINDING AFFINITY; BINDING SITE; CONTROLLED STUDY; CRYSTAL STRUCTURE; HUMAN; HUMAN CELL; MUTAGENESIS; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN LOCALIZATION; PROTEIN STRUCTURE; RECEPTOR BINDING; RESIDUE ANALYSIS;

CELL LINE; CRYSTALLOGRAPHY, X-RAY; HUMANS; PEPTIDE HORMONES; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RECEPTORS, PEPTIDE; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 78049446704     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M110.148221     Document Type: Article

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