Molecular and genetic basis of β2 -adrenergic receptor function

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Presentation transcript:

Molecular and genetic basis of β2 -adrenergic receptor function Stephen B. Liggett Journal of Allergy and Clinical Immunology Volume 104, Issue 2, Pages S42-S46 (August 1999) DOI: 10.1016/S0091-6749(99)70272-1 Copyright © 1999 Mosby, Inc. Terms and Conditions

Fig. 1 Primary amino-acid sequence and proposed membrane topography of the human β2 AR. The single letter amino acid nomenclature is used. Shown is the receptor that is termed wild-type . Journal of Allergy and Clinical Immunology 1999 104, S42-S46DOI: (10.1016/S0091-6749(99)70272-1) Copyright © 1999 Mosby, Inc. Terms and Conditions

Fig. 2 Proposed positioning of the R-isomer of the agonist isoproterenol in the binding pocket of the β2 AR. The interaction at Asn293 determines the stereoselectivity for R- versus S-isomer. (From Wieland K, Zuurmond HM, Krasel C, Izerman AP, Lohse MJ. Involvement of Asn-293 in stereospecific agonist recognition and in activation of the β2 -adrenergic receptor. Proc Natl Acad Sci USA 1996;93:9276-81. Copyright 1996 National Academy of Sciences, U.S.A.) Journal of Allergy and Clinical Immunology 1999 104, S42-S46DOI: (10.1016/S0091-6749(99)70272-1) Copyright © 1999 Mosby, Inc. Terms and Conditions

Fig. 3 Signaling of β2 AR in the absence of agonist. Chinese hamsters fibroblasts (CHW) expressing different levels of β2 AR (expressed as fmol per mg on the x-axis) were homogenized, and basal adenylyl cyclase activities were determined in membranes. As is shown, a direct relationship between expression and basal activity is present. Journal of Allergy and Clinical Immunology 1999 104, S42-S46DOI: (10.1016/S0091-6749(99)70272-1) Copyright © 1999 Mosby, Inc. Terms and Conditions

Fig. 4 Localization of polymorphisms at amino acid positions 16, 27, 34, and 164 of the receptor and 19 of the 5 ́-LC. Journal of Allergy and Clinical Immunology 1999 104, S42-S46DOI: (10.1016/S0091-6749(99)70272-1) Copyright © 1999 Mosby, Inc. Terms and Conditions