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A point mutation in the seventh hydrophobic domain of the α2 adrenergic receptor increases its affinity for a family of β receptor antagonists

Author
SURYANARAYANA, S1 ; DAUNT, D. A; VON ZASTROW, M; KOBILKA, B. K
[1] Stanford univ., Howard Hughes medical inst., Stanford CA 94305, United States
Source

The Journal of biological chemistry (Print). 1991, Vol 266, Num 23, pp 15488-15492 ; ref : 29 ref

CODEN
JBCHA3
ISSN
0021-9258
Scientific domain
Biochemistry, molecular biology, biophysics; Biotechnology
Publisher
American Society for Biochemistry and Molecular Biology, Bethesda, MD
Publication country
United States
Document type
Article
Language
English
Keyword (fr)
Capacité fixation Homme Immunofluorescence Récepteur α2-adrénergique Site fixation Spécificité substrat Séquence aminoacide Récepteur membranaire
Keyword (en)
Binding capacity Human Immunofluorescence α2-Adrenergic receptor Binding site Substrate specificity Aminoacid sequence Membrane receptor
Keyword (es)
Capacidad de fijación Hombre Inmunofluorescencia Receptor α2-adrenérgico Sitio fijación Especificidad sustrato Secuencia aminoácido Receptor membrana
Classification
Pascal
002 Biological and medical sciences / 002A Fundamental and applied biological sciences. Psychology / 002A04 Molecular and cellular biology / 002A04F Cell structures and functions / 002A04F03 Cell receptors / 002A04F03B Monoamines receptors (catecholamine, serotonine, histamine, acetylcholine)

Discipline
Molecular and cell biology
Origin
Inist-CNRS
Database
PASCAL
INIST identifier
4956297

Sauf mention contraire ci-dessus, le contenu de cette notice bibliographique peut être utilisé dans le cadre d’une licence CC BY 4.0 Inist-CNRS / Unless otherwise stated above, the content of this bibliographic record may be used under a CC BY 4.0 licence by Inist-CNRS / A menos que se haya señalado antes, el contenido de este registro bibliográfico puede ser utilizado al amparo de una licencia CC BY 4.0 Inist-CNRS

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