-
1
-
-
0027190359
-
Projection Structure of Rhodopsin
-
of outstanding interest, Direct information on the structure of a G protein coupled receptor, obtained by electron crystallography of two-dimensional crystals. The map at 9Ȧ resolution is interpreted as showing seven helices in projection.
-
(1993)
Nature
, vol.362
, pp. 770-772
-
-
Schertler1
Villa2
Henderson3
-
2
-
-
0027506471
-
The Probable Arrangement of the Helices in G Protein-Coupled Receptors
-
(1993)
EMBO J
, vol.12
, pp. 1693-1703
-
-
Baldwin1
-
3
-
-
0026496893
-
Thyrotropin-Releasing Hormone Binding to the Mouse Pituitary Receptor Does Not Involve Ionic Interactions. A Model for Neutral Peptide Binding to G Protein-Coupled Receptors
-
(1992)
J Biol Chem
, vol.267
, pp. 24413-24417
-
-
Perlman1
Nussenzveig2
Osman3
Gershengorn4
-
4
-
-
0026666733
-
Identification of Amino Acid Residues of Rat Angiotensin II Receptor for Ligand Binding by Site-Directed Mutagenesis
-
of special interest, Mutation Lys199Gln (V:6) strongly reduces binding of angiotensin II, as does replacement by glycine of each of four extracellular cysteines in the following positions: III:0, IV–V loop, amino-terminal region and the VI–VII loop.
-
(1992)
Biochem Biophys Res Commun
, vol.187
, pp. 1426-1431
-
-
Yamano1
Ohyama2
Chaki3
Guo4
Inagami5
-
6
-
-
0026548090
-
Histidine Residues Regulate the Transition of Photoexcited Rhodopsin to Its Active Conformation, Metarhodopsin II
-
of special interest, Mutation His211Phe/Cys (V:10) formed little or no metarhodopsin II at either extreme of pH. Histidine 211 must be in a position where protonation strongly stabilizes the metarhodopsin II conformation.
-
(1992)
Neuron
, vol.8
, pp. 465-472
-
-
Weitz1
Nathans2
-
7
-
-
0026707322
-
Cloning, Expression and Characterization of the Unique Bovine A1 Adenosine Receptor: Studies on the Ligand Binding Site by Site-Directed Mutagenesis
-
(1992)
J Biol Chem
, vol.267
, pp. 10764-10770
-
-
Olah1
Ren2
Ostrowski3
Jacobson4
Stiles5
-
8
-
-
0027533339
-
Functional Role of Proline and Tryptophan Residues Highly Conserved Among G Protein-Coupled Receptors Studied by Mutational Analysis of the m3 Muscarinic Receptor
-
of special interest, Mutations Trp503Phe (VI:16) and Pro201Ala (IV:20) show reduced binding of both agonists and antagonists. Mutations Trp192Phe (IV:11) and Pro242Ala (V:14) show essentially normal antagonist binding but reduced agonist binding. The Pro540Ala (VII:18) mutation yields normal antagonist affinity; it has increased affinity for agonists but impaired IP formation. The mutations Pro505Ala (VI:18) and Trp530Phe (VII:8) have no effect.
-
(1993)
EMBO J
, vol.12
, pp. 331-338
-
-
Wess1
Nanavati2
Vogel3
Maggio4
-
9
-
-
0026639831
-
Site-Directed Mutagenesis of the Rat m1 Muscarinic Acetylcholine Receptor. Role of Conserved Cysteines in Receptor Function
-
of special interest, Mutation Cys407Ser (VII:10) decreases carbachol affinity and decreases efficacy for stimulation of PI hydrolysis. Cys417Ser (VII:20) yields an increase in carbachol affinity. Neither mutation results in a change in affinity for antagonists. Mutation Cys98Ser (III:0) or Cys178Ser (in IV–V loop) probably produces an improperly folded protein as no binding can be detected.
-
(1992)
J Biol Chem
, vol.267
, pp. 11439-11448
-
-
Savarese1
Wang2
Fraser3
-
10
-
-
0026488456
-
The Role of Conserved Aspartate and Serine Residues in Ligand Binding and Function of the 5-HT1A Receptor: A Site-Directed Mutation Study
-
of special interest, Four separate mutations, Asp82Asn (II:14), Asp116Asn (III:7), Ser198Ala (V:6), Thr199Ala (V:7), produce receptors with wild-type affinity for the antagonist pindolol but with decreased affinity for serotonin. Serotonin stimulates GTPase activity in all four mutants, but less efficiently than in wild-type.
-
(1992)
FEBS Lett
, vol.312
, pp. 259-262
-
-
Ho1
Karschin2
Branchek3
Davidson4
Lester5
-
12
-
-
0027249759
-
+ Regulation of Agonist Binding but Does Not Alter Receptor-G Protein Association
-
+. The agonist affinity of the mutant protein is the same as that of wild-type protein, and it remains regulated by GTP analogs; this property differs from the consequences of the homologous mutation in other receptors.
-
(1993)
Mol Pharmacol
, vol.44
, pp. 380-384
-
-
Kong1
Raynor2
Yasuda3
Bell4
Reisine5
-
13
-
-
0027170277
-
The Regulation of the Binding Affinity of the Luteinizing Hormone/Choriogonadotropin Receptor by Sodium Ions Is Mediated by a Highly Conserved Aspartate Located in the Second Transmembrane Domain of G Protein-Coupled Receptors
-
+ on reducing the affinity of wild-type receptors. Aspartic acid 383 is also important for receptor activation.
-
(1993)
Mol Endocrinol
, vol.7
, pp. 767-775
-
-
Quintana1
Wang2
Ascoli3
-
15
-
-
0027296745
-
Amino Acid Substitutions at Position 312 in the Seventh Hydrophobic Segment of the β2-Adrenergic Receptor Modify Ligand Binding Specificity
-
(1993)
Mol Pharmacol
, vol.44
, pp. 111-114
-
-
Suryanarayana1
Kobilka2
-
16
-
-
0026661978
-
Constitutively Active Mutants of Rhodopsin
-
of special interest, Mutation of Lys296glu/Gly/Ala (VII:11), the lysine that normally binds 11-cis-retinal, or mutation of the counter-ion Glu113Gln (III:3), results in constitutively active opsin, activating transducin in the absence of retinal chromophore.
-
(1992)
Neuron
, vol.9
, pp. 719-725
-
-
Robinson1
Cohen2
Zhukovsky3
Oprian4
-
17
-
-
0026475571
-
Changing the Location of the Schiff Base Counterion in Rhodopsin
-
of special interest, The glutamate counter-ion can be moved from position 113 (III:3) to position 117 (III:7) without changing the wild-type spectral properties.
-
(1992)
Biochemistry
, vol.31
, pp. 10400-10405
-
-
Zhukovsky1
Robinson2
Oprian3
-
18
-
-
0027298812
-
Constitutive Activation of Opsin: Influence of Charge at Position 134 and Size at Position 296
-
of special interest, Mutation Glu134Gln (III:24) produces opsin that is active in the absence of chromophore, but mutation Glu134Asp does not. Twelve different mutations of Lys296 (VII:11), excluding mutation to arginine, produce constitutively active opsin.
-
(1993)
Biochemistry
, vol.32
, pp. 6111-6115
-
-
Cohen1
Yang2
Robinson3
Oprian4
-
19
-
-
0026780339
-
Structure and Function of Rhodopsin. Studies of the Interaction Between the Rhodopsin Cytoplasmic Domain and Transducin
-
of special interest, Mutations Glu134Gln/Asp (III:24) and Arg135Gln affect activation of transducin. The double mutant GluArg to AlaAla/ArgGlu fails to activate transducin. Both cytoplasmic loops III-IV and V-VI are required for transducin activation.
-
(1992)
J Biol Chem
, vol.267
, pp. 14767-14774
-
-
Franke1
Sakmar2
Graham3
Khorana4
-
20
-
-
0026661975
-
Introduction of Hydroxyl-Bearing Amino Acids Causes Bathochromic Spectral Shifts in Rhodopsin. Amino Acid Substitutions Responsible for Red-Green Color Pigment Spectral Tuning
-
of special interest, Three residues that are non-polar in rhodopsin and green colour pigment were mutated in turn to the polar residues present in red colour pigment. Phe261Tyr (VI:12) and Ala269Thr (VI:20) cause a significant red shift in the absorption maxima; Ala164Ser (IV:14) causes a slight effect. These three residues had been proposed as responsible for spectral tuning in earlier work.
-
(1992)
J Biol Chem
, vol.267
, pp. 9478-9480
-
-
Chan1
Lee2
Sakmar3
-
21
-
-
0027092318
-
Molecular basis for the species selectivity of the neurokinin-1 receptor antagonists CP-96,345 and RP67580.
-
of special interest, Substitution of Ile290Ser (VII:6) and Val116Leu (III:11) in human NK1 receptor is necessary and sufficient to produce antagonist binding properties of the rat receptor.
-
(1992)
J Biol Chem
, vol.267
, pp. 25668-25671
-
-
Fong1
Yu2
Strader3
-
22
-
-
0027080834
-
Cloning of two mouse genes encoding alpha 2-adrenergic receptor subtypes and identification of a single amino acid in the mouse alpha 2-C10 homolog responsible for an interspecies variation in antagonist binding.
-
(1992)
Mol Pharmacol
, vol.42
, pp. 16-27
-
-
Link1
Daunt2
Barsh3
Chruscinski4
Kobilka5
-
23
-
-
0027460624
-
A Single Amino Acid of the Cholecystokinin-B/Gastrin Receptor Determines Specificity for Non-Peptide Antagonists
-
(1993)
Nature
, vol.362
, pp. 348-350
-
-
Beinborn1
Lee2
McBride3
Quinn4
Kopin5
-
25
-
-
0027236371
-
The Fifth Transmembrane Segment of the Neuromedin B Receptor Is Critical for High Affinity Neuromedin B Binding
-
of special interest, Mutation Ile216 (V:6) to serine, the amino acid in the receptor for gastrin-releasing peptide, abolishes high affinity binding for neuromedin B and severely impairs the stimulation of IP production.
-
(1993)
J Biol Chem
, vol.268
, pp. 14622-14626
-
-
Fathi1
Benya2
Shapira3
Jensen4
Battey5
-
26
-
-
0027273840
-
Characterization of Mutant Rhodopsins Responsible for Autosomal Dominant Retinitis Pigmentosa. Mutations on the Cytoplasmic Surface Affect Transducin Activation
-
of special interest, Mutated rhodopsins Thr58Arg (I:21) or Arg135Leu/Trp (III:25) bind 11-cis-retinal to form pigments with normal absorbance maximum. Upon illumination they form spectral forms similar to metarhodopsin II, that are defective in activating guanine-nucleotide exchange by transducin.
-
(1993)
J Biol Chem
, vol.268
, pp. 9400-9404
-
-
Min1
Zvyaga2
Cypess3
Sakmar4
-
27
-
-
0027413475
-
Pigmentation Phenotypes of Variant Extension Locus Alleles Result from Point Mutations That Alter MSH Receptor Function
-
of special interest, Naturally occurring point mutation Glu92Lys (II:24) produces a receptor that is constitutively active and unresponsive to αMSH. Basal activity for adenylyl cyclase activity is increased by a factor of 4, to approximately 60% of the maximum response achieved by wild-type.
-
(1993)
Cell
, vol.72
, pp. 827-834
-
-
Robbins1
Nadeau2
Johnson3
Kelly4
Roselli-Rehfuss5
Baack6
Mountjoy7
Cone8
-
28
-
-
0027369421
-
Somatic Mutations in the Thyrotropin Receptor Gene Cause Hyperfunctioning Thyroid Adenomas
-
of special interest, One of the point mutations was Ala623Ile (VI:2) and the other was Asp619Gly. For cAMP accumulation, both mutated receptors showed increased basal rates (by factors of 3 and 2) but they remained responsive to agonist with wild-type maximum response. For IP accumulation, neither mutated receptor had an increased basal level of activity.
-
(1993)
Nature
, vol.365
, pp. 649-651
-
-
Parma1
Duprez2
Van Sande3
Cochaux4
Gervy5
Mockel6
Dumont7
Vassart8
-
29
-
-
0027372340
-
A Constitutively Activating Mutation of the Luteinizing Hormone Receptor in Familial Male Precocious Puberty
-
of special interest, The point mutation Asp578Gly (VI:12) leads to increased cAMP production in the absence of agonist. Basal level of cAMP production rose by a factor 4, to approximately 30% of the wild-type maximum response. The mutated receptor still responded to agonist with a normal level of maximum response.
-
(1993)
Nature
, vol.365
, pp. 652-654
-
-
Shenker1
Laue2
Kosugi3
Merendino4
Minegishi5
Cutler6
-
30
-
-
0027248024
-
Heterozygous Missense Mutation in the Rhodopsin Gene as a Cause of Congenital Night Blindness
-
of special interest, The point mutation was Ala292Glu (VII:7). In vitro studies showed that the mutated rhodopsin activates transducin in the absence of 11-cis-retinal. In the presence of retinal it resembles wild-type in activating transducin in a light-dependent manner.
-
(1993)
Nature Genetics
, vol.4
, pp. 280-283
-
-
Dryja1
Berson2
Rao3
Oprian4
-
31
-
-
0026592357
-
Constitutive Activation of the α1b-Adrenergic Receptor by All Amino Acid Substitutions at a Single Site. Evidence for a Region Which Constrains Receptor Activation
-
of special interest, All 19 possible substitutions of Ala293 (VI:2) confer constitutive activity and higher affinity for agonists. Basal levels of IP are not correlated with an increase in affinity. All mutated receptors are able to respond to epinephrine.
-
(1992)
J Biol Chem
, vol.267
, pp. 1430-1433
-
-
Kjelsberg1
Cotecchia2
Ostrowski3
Caron4
Lefkowitz5
-
32
-
-
0027296623
-
Constitutively Active Mutants of the α2-Adrenergic Receptor
-
of special interest, Five different substitutions (Phe, Ala, Cys, Glu, Lys) for threonine at position VI:2 led to constitutively active mutants with increased affinity for agonist but not for antagonists. Stimulation by agonists occurred above the basal level, to approximately the same maximum level as for wild-type.
-
(1993)
J Biol Chem
, vol.268
, pp. 16483-16487
-
-
Ren1
Kurose2
Lefkowitz3
Cotecchia4
-
33
-
-
0026464910
-
Mutation of Alanine 623 in the Third Cytoplasmic Loop of the Rat Thyrotropin (TSH) Receptor Results in a Loss in the Phosphoinositide but not cAMP Signal Induced by TSH and Receptor Autoantibodies
-
(1992)
J Biol Chem
, vol.267
, pp. 24153-24156
-
-
Kosugi1
Okajima2
Ban3
Hidaka4
Shenker5
Kohn6
-
34
-
-
0027043104
-
Localization of agonist and antagonist binding domains of the human neurokinin-1 receptor.
-
of special interest, Separate mutations of Asn23Thr, Gln24Ala, Phe25Ala in the amino-terminal segment and of His108Gln (III:3) and Asn96Ser in the loop II–III region greatly reduce the binding of all three tachykinin peptides. Also, loops IV–V and VI–VII, and the transmembrane domain, are implicated in ligand binding.
-
(1992)
J Biol Chem
, vol.267
, pp. 25664-25667
-
-
Fong1
Huang2
Strader3
-
35
-
-
0026454825
-
The Extracellular Domain of the Neurokinin-1 Receptor Is Required for High-Affinity Binding of Peptides
-
of special interest, Substitution of amino acids in the amino-terminal sequence alters the binding affinity for peptides but not for a non-peptide antagonist. Also mutation Val97Glu in loop II–III alters the binding affinity for neurokinin-B. The authors suggest that the conserved carboxy-terminal part of tachykinin peptides interacts with the amino terminus of the receptors.
-
(1992)
Biochemistry
, vol.31
, pp. 11806-11811
-
-
Fong1
Yu2
Huang3
Strader4
-
36
-
-
0026779423
-
Delineation of Structural Domains Involved in the Subtype Specificity of Tachykinin Receptors Through Chimeric Formation of Substance P/Subtance K Receptors
-
•].
-
(1992)
EMBO J
, vol.11
, pp. 3585-3591
-
-
Yokota1
Akazawa2
Ohkubo3
Nakanishi4
-
37
-
-
0028351937
-
Structure and Function in Rhodopsin: Replacement by Alanines of the Intradiscal Cysteines 110 and 187, Components of a Conserved Disulphide Bond in Rhodopsin, Affects the Light-Activated Meta II State
-
of special interest, in press, The double mutation Cys110Ala (III:0)/Cys187Ala(IV–V loop) produces correctly folded opsin that binds 11-cis-retinal normally. The Meta II photo-intermediate of the mutant is less stable than that of wild-type rhodopsin. The disulphide bond is therefore important in stabilizing the Meta II structure and its coupling to transducin activation, but is not necessary for the ground-state structure.
-
(1994)
Proc Natl Acad Sci USA
-
-
Davidson1
Khorana2
-
38
-
-
0027080608
-
Domains for G-Protein Coupling in Angiotensin II Receptor Type I: Studies by Site-Directed Mutagenesis
-
3 formation. These are Asp-Arg-Tyr (III:24–26) to Gly-Gly-Ala; removal of charges in carboxy-terminal regions of loop III–IV or loop V–VI; and deletion of the carboxyl terminus starting from three residues after the end of helix VII.
-
(1992)
Biochem Biophys Res Commun
, vol.189
, pp. 677-683
-
-
Ohyama1
Yamano2
Chaki3
Kondo4
Inagami5
-
39
-
-
0027328071
-
Charged Amino Acids Required for Signal Transduction by the m3 Muscarinic Acetylcholine Receptor
-
of special interest, Two clusters of charged residues near transmembrane segments V and VI are required for normal signalling. A V–VI loop reduced in length to 22 amino acids yields an active receptor, provided the two charged sequences at either end are present.
-
(1993)
EMBO J
, vol.12
, pp. 3809-3815
-
-
Kunkel1
Peralta2
-
40
-
-
0027250914
-
Substitutions of Different Regions of the Third Cytoplasmic Loop of the Thyrotropin (TSH) Receptor Have Selective Effects on Constitutive, TSH-, and TSH Receptor Autoantibody-Stimulated Phosphoinositide and 3′,5′-Cyclic Adenosine Monophosphate Signal Generation
-
2 signal, but not for the induction of the cAMP signal. They are also important for regulation of constitutive cAMP levels.
-
(1993)
Mol Endocrinol
, vol.7
, pp. 1009-1020
-
-
Kosugi1
Okajima2
Ban3
Hidaka4
Shenker5
Kohn6
-
41
-
-
0027513982
-
A Mutation-Induced State of the β2-Adrenergic Receptor. Extending the Ternary Complex Model
-
of outstanding interest, Replacement of the carboxy-terminal part of the V–VI loop of the β2 receptor with the sequence of the α1b receptor leads to agonist-independent activation of adenylyl cyclase. The equations that describe receptor equilibria are reformulated to account for the phenomenon of constitutive activation in mutated receptors.
-
(1993)
J Biol Chem
, vol.268
, pp. 4625-4636
-
-
Samama1
Cotecchia2
Costa3
Lefkowitz4
-
42
-
-
0027465919
-
Palmitoylation of Bovine Opsin and Its Cysteine Mutants in COS Cells
-
of special interest, Mutations Cys322Ser and/or Cys323Ser, resulting in complete abolition of palmitoylation, do not affect 11-cis-retinal binding or light-dependent binding and activation of transducin. These conclusions differ from an earlier report which stated that removal of palmitate with hydroxylamine increases the light-dependent activation of transducin.
-
(1993)
Proc Natl Acad Sci USA
, vol.90
, pp. 40-44
-
-
Karnik1
Ridge2
Bhattacharya3
Khorana4
-
43
-
-
0027401994
-
Mutations of the α2a Adrenergic Receptor That Eliminate Detectable Palmitoylation Do Not Perturb Receptor G Protein Coupling
-
s, in which attenuation of coupling was found.
-
(1993)
J Biol Chem
, vol.268
, pp. 8003-8011
-
-
Kennedy1
Limbird2
|