The extracellular domains of ErbB3 retain high ligand binding affinity at endosome pH and in the locked conformation

Biochemistry

Volumn 44, Issue 48, 2005, Pages 15842-15857

  Kani, Kian ^b   Park, Euisun ^b   Landgraf, Ralf ^a,b,c  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c NONE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; CONFORMATIONS; CRYSTAL STRUCTURE; MOLECULAR STRUCTURE; MUTAGENESIS; PH EFFECTS;

AFFINITY STATES; EXTRACELLULAR DOMAINS; LIGAND BINDING; PICOMOLAR BINDING;

CYTOLOGY;

EPIDERMAL GROWTH FACTOR RECEPTOR 3; MUTANT PROTEIN;

ARTICLE; BINDING AFFINITY; BINDING SITE; COMPARATIVE STUDY; COMPLEX FORMATION; CRYSTAL STRUCTURE; DIMERIZATION; ENDOSOME; LIGAND BINDING; MOLECULAR MODEL; PH; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; WILD TYPE;

AMINO ACID SUBSTITUTION; ANIMALS; DISULFIDES; DROSOPHILA; ENDOSOMES; HYDROGEN-ION CONCENTRATION; LIGANDS; MODELS, MOLECULAR; MUTATION; NEUREGULIN-1; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; RECEPTOR, ERBB-3; SURFACE PLASMON RESONANCE;

EID: 28544448126     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0515220     Document Type: Article

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