Mutation of a highly conserved aspartic acid in the beta2 adrenergic receptor: constitutive activation, structural instability, and conformational rearrangement of transmembrane segment 6.
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P Ghanouni | G. Liapakis | J. Javitch | S. Rasmussen | P. Ghanouni | U. Gether | S G Rasmussen | A D Jensen | G Liapakis | J A Javitch | U Gether | A. Jensen | Søren G. F. Rasmussen
[1] Gebhard F. X. Schertler,et al. Arrangement of rhodopsin transmembrane α-helices , 1997, Nature.
[2] B. Kobilka,et al. Construction and expression of chimeric receptors to understand the structure-function relationships in adrenergic receptors , 1991 .
[3] C. Londos,et al. A highly sensitive adenylate cyclase assay. , 1974, Analytical biochemistry.
[4] J. Venter,et al. Site-directed mutagenesis of human beta-adrenergic receptors: substitution of aspartic acid-130 by asparagine produces a receptor with high-affinity agonist binding that is uncoupled from adenylate cyclase. , 1988, Proceedings of the National Academy of Sciences of the United States of America.
[5] H Weinstein,et al. Agonists induce conformational changes in transmembrane domains III and VI of the β2 adrenoceptor , 1997, The EMBO journal.
[6] J. Ballesteros,et al. [19] Integrated methods for the construction of three-dimensional models and computational probing of structure-function relations in G protein-coupled receptors , 1995 .
[7] H. Khorana,et al. Structure and function in rhodopsin: rhodopsin mutants with a neutral amino acid at E134 have a partially activated conformation in the dark state. , 1997, Proceedings of the National Academy of Sciences of the United States of America.
[8] Robert P. Millar,et al. Functional Microdomains in G-protein-coupled Receptors , 1998, The Journal of Biological Chemistry.
[9] J. Javitch,et al. A cysteine residue in the third membrane-spanning segment of the human D2 dopamine receptor is exposed in the binding-site crevice. , 1994, Proceedings of the National Academy of Sciences of the United States of America.
[10] M. Birnbaumer,et al. Nephrogenic diabetes insipidus. A V2 vasopressin receptor unable to stimulate adenylyl cyclase. , 1993, The Journal of biological chemistry.
[11] W. C. Probst,et al. Sequence alignment of the G-protein coupled receptor superfamily. , 1992, DNA and cell biology.
[12] H. Khorana,et al. Requirement of Rigid-Body Motion of Transmembrane Helices for Light Activation of Rhodopsin , 1996, Science.
[13] M. Caron,et al. Constitutive activation of the alpha 1B-adrenergic receptor by all amino acid substitutions at a single site. Evidence for a region which constrains receptor activation. , 1992, The Journal of biological chemistry.
[14] Brian K. Kobilka,et al. Structural Instability of a Constitutively Active G Protein-coupled Receptor , 1997, The Journal of Biological Chemistry.
[15] J. Baldwin,et al. Arrangement of rhodopsin transmembrane alpha-helices. , 1997, Nature.
[16] A. Scheer,et al. Constitutively active mutants of the alpha 1B‐adrenergic receptor: role of highly conserved polar amino acids in receptor activation. , 1996, The EMBO journal.
[17] M. Grossmann,et al. G Protein-coupled Receptors , 1998, The Journal of Biological Chemistry.
[18] D. Oprian,et al. A general method for mapping tertiary contacts between amino acid residues in membrane-embedded proteins. , 1995, Biochemistry.
[19] T. S. Kobilka,et al. Enhancement of membrane insertion and function in a type IIIb membrane protein following introduction of a cleavable signal peptide. , 1992, The Journal of biological chemistry.
[20] D. Perez,et al. Activation of the α1b-Adrenergic Receptor Is Initiated by Disruption of an Interhelical Salt Bridge Constraint* , 1996, The Journal of Biological Chemistry.
[21] T. Schwartz,et al. Constitutive activity of glucagon receptor mutants. , 1998, Molecular endocrinology.
[22] Jonathan A Javitch,et al. Mapping the binding-site crevice of the dopamine D2 receptor by the substituted-cysteine accessibility method , 1995, Neuron.
[23] K. Fahmy,et al. A conserved carboxylic acid group mediates light-dependent proton uptake and signaling by rhodopsin. , 1994, The Journal of biological chemistry.
[24] E. Hulme,et al. The role of the aspartate-arginine-tyrosine triad in the m1 muscarinic receptor: mutations of aspartate 122 and tyrosine 124 decrease receptor expression but do not abolish signaling. , 1997, Molecular pharmacology.
[25] J. Shafer,et al. Reactivity of small thiolate anions and cysteine-25 in papain toward methyl methanethiosulfonate. , 1986, Biochemistry.
[26] B. Kobilka,et al. Fluorescent labeling of purified beta 2 adrenergic receptor. Evidence for ligand-specific conformational changes. , 1995, The Journal of biological chemistry.
[27] O. Lichtarge,et al. Rhodopsin activation blocked by metal-ion-binding sites linking transmembrane helices C and F , 1996, Nature.
[28] R. Lefkowitz,et al. A mutation-induced activated state of the beta 2-adrenergic receptor. Extending the ternary complex model. , 1993, The Journal of biological chemistry.
[29] P. Chidiac,et al. Inverse agonist activity of beta-adrenergic antagonists. , 1994, Molecular pharmacology.
[30] A. Scheer,et al. The activation process of the alpha1B-adrenergic receptor: potential role of protonation and hydrophobicity of a highly conserved aspartate. , 1997, Proceedings of the National Academy of Sciences of the United States of America.
[31] T. Sakmar,et al. Characterization of mutant rhodopsins responsible for autosomal dominant retinitis pigmentosa. Mutations on the cytoplasmic surface affect transducin activation. , 1993, The Journal of biological chemistry.
[32] D. Oprian,et al. Constitutive activation of opsin: influence of charge at position 134 and size at position 296. , 1993, Biochemistry.
[33] T. Schwartz,et al. Biosynthesis of peptide precursors and protease inhibitors using new constitutive and inducible eukaryotic expression vectors , 1990, FEBS letters.
[34] J. Javitch,et al. Constitutive Activation of the β2 Adrenergic Receptor Alters the Orientation of Its Sixth Membrane-spanning Segment* , 1997, The Journal of Biological Chemistry.
[35] J. Baldwin,et al. An alpha-carbon template for the transmembrane helices in the rhodopsin family of G-protein-coupled receptors. , 1997, Journal of molecular biology.
[36] A. Karlin,et al. Electrostatic potential of the acetylcholine binding sites in the nicotinic receptor probed by reactions of binding-site cysteines with charged methanethiosulfonates. , 1994, Biochemistry.
[37] K. Nakanishi,et al. Partial Agonist Activity of 11-cis-Retinal in Rhodopsin Mutants* , 1997, The Journal of Biological Chemistry.
[38] Gebhard F. X. Schertler,et al. Projection structure of rhodopsin , 1993, Nature.
[39] B. Kobilka,et al. G Protein-coupled Receptors , 1998, The Journal of Biological Chemistry.
[40] C. Strader,et al. Structure and function of G protein-coupled receptors. , 1994, Annual review of biochemistry.