Crystal structure of an affinity-matured prolactin complexed to its dimerized receptor reveals the topology of hormone binding site 2

Journal of Biological Chemistry

Volumn 285, Issue 11, 2010, Pages 8422-8433

  Broutin, Isabelle ^a   Jomain, Jean Baptiste ^b,c   Tallet, Estelle ^b,c   Van Agthoven, Jan ^a   Raynal, Bertrand ^a,d   Hoos, Sylviane ^a,d   Kragelund, Birthe B ^e   Kelly, Paul A ^b,c   Ducruix, Arnaud ^a   England, Patrick ^a,d   Goffin, Vincent ^b,c  

^a CNRS   (France)

^b INSERM   (France)

^c UNIVERSITÉ PARIS DESCARTES   (France)

^d INSTITUT PASTEUR   (France)

^e UNIVERSITY OF COPENHAGEN   (Denmark)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; COMPLEX NETWORKS; DISEASES; HYDROGEN BONDS; LIGANDS; MOLECULAR INTERACTIONS;

HORMONE-BINDING SITE; HYDROGEN BOND NETWORKS; INTERACTION MODEL; MOLECULAR MECHANISM; PROSTATE CANCERS; SITE DIRECTED MUTAGENESIS; STRUCTURAL COMPONENT; THERAPEUTIC POTENTIALS;

CRYSTAL STRUCTURE;

GLYCINE; LIGAND; PLACENTA LACTOGEN; PROLACTIN; PROLACTIN DERIVATIVE; PROLACTIN RECEPTOR; RECOMBINANT PROTEIN;

AMINO TERMINAL SEQUENCE; ARTICLE; BINDING AFFINITY; COMPLEX FORMATION; CONTROLLED STUDY; CRYSTAL STRUCTURE; DIMERIZATION; HYDROGEN BOND; PRIORITY JOURNAL; RECEPTOR BINDING; SITE DIRECTED MUTAGENESIS; AMINO ACID SEQUENCE; ANIMAL; BINDING SITE; CHEMISTRY; CRYSTALLOGRAPHY; DRUG DESIGN; GENETICS; HUMAN; METABOLISM; MOLECULAR GENETICS; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; RAT; SHEEP; STRUCTURE ACTIVITY RELATION; SURFACE PLASMON RESONANCE; X RAY DIFFRACTION;

OVIS;

AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CRYSTALLOGRAPHY; DIMERIZATION; DRUG DESIGN; GLYCINE; HUMANS; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PLACENTAL LACTOGEN; PROLACTIN; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RATS; RECEPTORS, PROLACTIN; RECOMBINANT PROTEINS; SHEEP; STRUCTURE-ACTIVITY RELATIONSHIP; SURFACE PLASMON RESONANCE; X-RAY DIFFRACTION;

EID: 77950882862     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.089128     Document Type: Article

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