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Volumn 6, Issue 2, 1994, Pages 180-190

Structure and function of receptors coupled to G proteins

Author keywords

[No Author keywords available]

Indexed keywords

GUANINE NUCLEOTIDE BINDING PROTEIN; MEMBRANE RECEPTOR; RECEPTOR; RHODOPSIN;

EID: 0028227013     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/0955-0674(94)90134-1     Document Type: Article
Times cited : (342)

References (43)
  • 1
    • 0027190359 scopus 로고
    • 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 scopus 로고
    • The Probable Arrangement of the Helices in G Protein-Coupled Receptors
    • (1993) EMBO J , vol.12 , pp. 1693-1703
    • Baldwin1
  • 3
    • 0026496893 scopus 로고
    • 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 scopus 로고
    • 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 scopus 로고
    • 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 scopus 로고
    • 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 scopus 로고
    • 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 scopus 로고
    • 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 scopus 로고
    • 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 scopus 로고
    • + 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 scopus 로고
    • 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 scopus 로고
    • 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 scopus 로고
    • 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 scopus 로고
    • 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 scopus 로고
    • 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 scopus 로고
    • 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 scopus 로고
    • 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 scopus 로고
    • 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 scopus 로고
    • 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 scopus 로고
    • 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 scopus 로고
    • 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 scopus 로고
    • 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 scopus 로고
    • 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 scopus 로고
    • 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 scopus 로고
    • 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 scopus 로고
    • 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 scopus 로고
    • 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 scopus 로고
    • 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 scopus 로고
    • 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 scopus 로고
    • 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 scopus 로고
    • 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 scopus 로고
    • 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 scopus 로고
    • 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 scopus 로고
    • 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 scopus 로고
    • 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 scopus 로고
    • 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 scopus 로고
    • 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 scopus 로고
    • 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 scopus 로고
    • 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


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