메뉴 건너뛰기




Volumn 70, Issue 1, 2006, Pages 206-213

Possible endogenous agonist mechanism for the activation of secretin family G protein-coupled receptors

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; ASPARTIC ACID; BENZOYLALANYLALANYL DEXTRO TRYPTOPHYLPHENYLALANYL DEXTRO PROLYLPROLYLNORLEUCINAMIDE; CALCITONIN RECEPTOR; CYCLIC AMP; CYCLOPEPTIDE; CYSTEINE; DOCKING PROTEIN; EPITOPE; FATTY ACID; GUANINE NUCLEOTIDE BINDING PROTEIN; LIGAND; MEMBRANE PROTEIN; SECRETIN; SYNTHETIC PEPTIDE; VASOACTIVE INTESTINAL POLYPEPTIDE;

EID: 33745267721     PISSN: 0026895X     EISSN: 15210111     Source Type: Journal    
DOI: 10.1124/mol.105.021840     Document Type: Article
Times cited : (37)

References (35)
  • 1
    • 0033784976 scopus 로고    scopus 로고
    • Structural insights into the amino-terminus of the secretin receptor: I. Status of cysteine and cystine residues
    • Asmann YW, Dong M, Ganguli S, Hadac EM, and Miller LJ (2000) Structural insights into the amino-terminus of the secretin receptor: I. Status of cysteine and cystine residues. Mol Pharmacol 58:911-919.
    • (2000) Mol Pharmacol , vol.58 , pp. 911-919
    • Asmann, Y.W.1    Dong, M.2    Ganguli, S.3    Hadac, E.M.4    Miller, L.J.5
  • 2
    • 0032575523 scopus 로고    scopus 로고
    • Parathyroid hormone-receptor interactions identified directly by photocross-linking and molecular modeling studies
    • Bisello A, Adams AE, Mierke DF, Pellegrini M, Rosenblatt M, Suva LJ, and Chorev M (1998) Parathyroid hormone-receptor interactions identified directly by photocross-linking and molecular modeling studies. J Biol Chem 273:22498-22505.
    • (1998) J Biol Chem , vol.273 , pp. 22498-22505
    • Bisello, A.1    Adams, A.E.2    Mierke, D.F.3    Pellegrini, M.4    Rosenblatt, M.5    Suva, L.J.6    Chorev, M.7
  • 3
    • 0028857383 scopus 로고
    • Highly conserved aspartate 68, tryptophane 73 and glycine 109 in the N-terminal extracellular domain of the human VIP receptor are essential for its ability to bind VIP
    • Couvineau A, Gaudin P, Maoret JJ, Rouyer-Fessard C, Nicole P, and Laburthe M (1995) Highly conserved aspartate 68, tryptophane 73 and glycine 109 in the N-terminal extracellular domain of the human VIP receptor are essential for its ability to bind VIP. Biochem Biophys Res Commun 206:246-252.
    • (1995) Biochem Biophys Res Commun , vol.206 , pp. 246-252
    • Couvineau, A.1    Gaudin, P.2    Maoret, J.J.3    Rouyer-Fessard, C.4    Nicole, P.5    Laburthe, M.6
  • 4
    • 0034714227 scopus 로고    scopus 로고
    • Identification of two pairs of spatially approximated residues within the carboxyl terminus of secretin and its receptor
    • Dong M, Asmann YW, Zang M, Pinon DI, and Miller LJ (2000) Identification of two pairs of spatially approximated residues within the carboxyl terminus of secretin and its receptor. J Biol Chem 275:26032-26039.
    • (2000) J Biol Chem , vol.275 , pp. 26032-26039
    • Dong, M.1    Asmann, Y.W.2    Zang, M.3    Pinon, D.I.4    Miller, L.J.5
  • 5
    • 1642494670 scopus 로고    scopus 로고
    • Spatial approximation between the amino terminus of a peptide agonist and the top of the sixth transmembrane segment of the secretin receptor
    • Dong M, Li Z, Pinon DI, Lybrand TP, and Miller LJ (2004a) Spatial approximation between the amino terminus of a peptide agonist and the top of the sixth transmembrane segment of the secretin receptor. J Biol Chem 279:2894-2903.
    • (2004) J Biol Chem , vol.279 , pp. 2894-2903
    • Dong, M.1    Li, Z.2    Pinon, D.I.3    Lybrand, T.P.4    Miller, L.J.5
  • 6
    • 0347951400 scopus 로고    scopus 로고
    • Spatial approximation between two residues in the mid-region of secretin and the amino terminus of its receptor. Incorporation of seven sets of such constraints into a three-dimensional model of the agonist-bound secretin receptor
    • Dong M, Li Z, Zang M, Pinon DI, Lybrand TP, and Miller LJ (2003) Spatial approximation between two residues in the mid-region of secretin and the amino terminus of its receptor. Incorporation of seven sets of such constraints into a three-dimensional model of the agonist-bound secretin receptor. J Biol Chem 278:48300-48312.
    • (2003) J Biol Chem , vol.278 , pp. 48300-48312
    • Dong, M.1    Li, Z.2    Zang, M.3    Pinon, D.I.4    Lybrand, T.P.5    Miller, L.J.6
  • 7
    • 0346463044 scopus 로고    scopus 로고
    • Importance of the amino terminus in secretin family G protein-coupled receptors: Intrinsic photoaffinity labeling establishes initial docking constraints for the calcitonin receptor
    • Dong M, Pinon DI, Cox RF, and Miller LJ (2004b) Importance of the amino terminus in secretin family G protein-coupled receptors: intrinsic photoaffinity labeling establishes initial docking constraints for the calcitonin receptor. J Biol Chem 279:1167-1175.
    • (2004) J Biol Chem , vol.279 , pp. 1167-1175
    • Dong, M.1    Pinon, D.I.2    Cox, R.F.3    Miller, L.J.4
  • 8
    • 3843090641 scopus 로고    scopus 로고
    • Molecular approximation between a residue in the amino-terminal region of calcitonin and the third extracellular loop of the class B G protein-coupled calcitonin receptor
    • Dong M, Pinon DI, Cox RF, and Miller LJ (2004c) Molecular approximation between a residue in the amino-terminal region of calcitonin and the third extracellular loop of the class B G protein-coupled calcitonin receptor. J Biol Chem 279:31177-31182.
    • (2004) J Biol Chem , vol.279 , pp. 31177-31182
    • Dong, M.1    Pinon, D.I.2    Cox, R.F.3    Miller, L.J.4
  • 9
    • 22444436330 scopus 로고    scopus 로고
    • Insights into the structure and molecular basis of ligand docking to the g protein-coupled secretin receptor using charge-modified amino-terminal agonist probes
    • Dong M, Pinon DI, and Miller LJ (2005) Insights into the structure and molecular basis of ligand docking to the g protein-coupled secretin receptor using charge-modified amino-terminal agonist probes. Mol Endocrinol 19:1821-1836.
    • (2005) Mol Endocrinol , vol.19 , pp. 1821-1836
    • Dong, M.1    Pinon, D.I.2    Miller, L.J.3
  • 10
    • 0033516657 scopus 로고    scopus 로고
    • Identification of an interaction between residue 6 of the natural peptide ligand and a distinct residue within the amino-terminal tail of the secretin receptor
    • Dong M, Wang Y, Hadac EM, Pinon DI, Holicky E, and Miller LJ (1999a) Identification of an interaction between residue 6 of the natural peptide ligand and a distinct residue within the amino-terminal tail of the secretin receptor. J Biol Chem 274:19161-19167.
    • (1999) J Biol Chem , vol.274 , pp. 19161-19167
    • Dong, M.1    Wang, Y.2    Hadac, E.M.3    Pinon, D.I.4    Holicky, E.5    Miller, L.J.6
  • 11
    • 0033534683 scopus 로고    scopus 로고
    • Demonstration of a direct interaction between residue 22 in the carboxyl-terminal half of secretin and the amino-terminal tail of the secretin receptor using photoaffinity labeling
    • Dong M, Wang Y, Pinon DI, Hadac EM, and Miller LJ (1999b) Demonstration of a direct interaction between residue 22 in the carboxyl-terminal half of secretin and the amino-terminal tail of the secretin receptor using photoaffinity labeling. J Biol Chem 274:903-909.
    • (1999) J Biol Chem , vol.274 , pp. 903-909
    • Dong, M.1    Wang, Y.2    Pinon, D.I.3    Hadac, E.M.4    Miller, L.J.5
  • 12
    • 0036843029 scopus 로고    scopus 로고
    • Interaction among four residues distributed through the secretin pharmacophore and a focused region of the secretin receptor amino terminus
    • Dong M, Zang M, Pinon DI, Li Z, Lybrand TP, and Miller LJ (2002) Interaction among four residues distributed through the secretin pharmacophore and a focused region of the secretin receptor amino terminus. Mol Endocrinol 16:2490-2501.
    • (2002) Mol Endocrinol , vol.16 , pp. 2490-2501
    • Dong, M.1    Zang, M.2    Pinon, D.I.3    Li, Z.4    Lybrand, T.P.5    Miller, L.J.6
  • 13
    • 0032410647 scopus 로고    scopus 로고
    • Protean effects of a natural peptide agonist of the G protein-coupled secretin receptor demonstrated by receptor mutagenesis
    • Ganguli SC, Park CG, Holtmann MH, Hadac EM, Kenakin TP, and Miller LJ (1998) Protean effects of a natural peptide agonist of the G protein-coupled secretin receptor demonstrated by receptor mutagenesis. J Pharmacol Exp Ther 286:593-598.
    • (1998) J Pharmacol Exp Ther , vol.286 , pp. 593-598
    • Ganguli, S.C.1    Park, C.G.2    Holtmann, M.H.3    Hadac, E.M.4    Kenakin, T.P.5    Miller, L.J.6
  • 14
    • 0027265595 scopus 로고
    • GHRH receptor of little mice contains a missense mutation in the extracellular domain that disrupts receptor function
    • Godfrey P, Rahal JO, Beamer WG, Copeland NG, Jenkins NA, and Mayo KE (1993) GHRH receptor of little mice contains a missense mutation in the extracellular domain that disrupts receptor function. Nat Genet 4:227-232.
    • (1993) Nat Genet , vol.4 , pp. 227-232
    • Godfrey, P.1    Rahal, J.O.2    Beamer, W.G.3    Copeland, N.G.4    Jenkins, N.A.5    Mayo, K.E.6
  • 15
  • 16
    • 4444351153 scopus 로고    scopus 로고
    • NMR structure and peptide hormone binding site of the first extracellular domain of a type B1 G protein-coupled receptor
    • Grace CR, Perrin MH, DiGruccio MR, Miller CL, Rivier JE, Vale WW, and Riek R (2004) NMR structure and peptide hormone binding site of the first extracellular domain of a type B1 G protein-coupled receptor. Proc Natl Acad Sci USA 101:12836-12841.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 12836-12841
    • Grace, C.R.1    Perrin, M.H.2    DiGruccio, M.R.3    Miller, C.L.4    Rivier, J.E.5    Vale, W.W.6    Riek, R.7
  • 17
    • 0029791442 scopus 로고    scopus 로고
    • Relationship between native and recombinant cholecystokinin receptors: Role of differential glycosylation
    • Hadac EM, Ghanekar DV, Holicky EL, Pinon DI, Dougherty RW, and Miller LJ (1996) Relationship between native and recombinant cholecystokinin receptors: role of differential glycosylation. Pancreas 13:130-139.
    • (1996) Pancreas , vol.13 , pp. 130-139
    • Hadac, E.M.1    Ghanekar, D.V.2    Holicky, E.L.3    Pinon, D.I.4    Dougherty, R.W.5    Miller, L.J.6
  • 18
    • 15844385219 scopus 로고    scopus 로고
    • Multiple extracellular loop domains contribute critical determinants for agonist binding and activation of the secretin receptor
    • Holtmann MH, Ganguli S, Hadac EM, Dolu V, and Miller LJ (1996) Multiple extracellular loop domains contribute critical determinants for agonist binding and activation of the secretin receptor. J Biol Chem 271:14944-14949.
    • (1996) J Biol Chem , vol.271 , pp. 14944-14949
    • Holtmann, M.H.1    Ganguli, S.2    Hadac, E.M.3    Dolu, V.4    Miller, L.J.5
  • 19
    • 0029043789 scopus 로고
    • Critical contributions of aminoterminal extracellular domains in agonist binding and activation of secretin and vasoactive intestinal polypeptide receptors. Studies of chimeric receptors
    • Holtmann MH, Hadac EM, and Miller LJ (1995) Critical contributions of aminoterminal extracellular domains in agonist binding and activation of secretin and vasoactive intestinal polypeptide receptors. Studies of chimeric receptors. J Biol Chem 270:14394-14398.
    • (1995) J Biol Chem , vol.270 , pp. 14394-14398
    • Holtmann, M.H.1    Hadac, E.M.2    Miller, L.J.3
  • 20
    • 0032504237 scopus 로고    scopus 로고
    • G protein-coupled receptors. I. Diversity of receptor-ligand interactions
    • Ji TH, Grossmann M, and Ji I (1998) G protein-coupled receptors. I. Diversity of receptor-ligand interactions. J Biol Chem 273:17299-17302.
    • (1998) J Biol Chem , vol.273 , pp. 17299-17302
    • Ji, T.H.1    Grossmann, M.2    Ji, I.3
  • 22
    • 0029943079 scopus 로고    scopus 로고
    • Agonist recognition by proteinase-activated receptor 2 and thrombin receptor. Importance of extracellular loop interactions for receptor function
    • Lerner DJ, Chen M, Tram T, and Coughlin SR (1996) Agonist recognition by proteinase-activated receptor 2 and thrombin receptor. Importance of extracellular loop interactions for receptor function. J Biol Chem 271:13943-13947.
    • (1996) J Biol Chem , vol.271 , pp. 13943-13947
    • Lerner, D.J.1    Chen, M.2    Tram, T.3    Coughlin, S.R.4
  • 23
    • 0036829810 scopus 로고    scopus 로고
    • The kinetics of the removal of the N-methyltrityl (Mtt) group during the synthesis of branched peptides
    • Li D and Elbert DL (2002) The kinetics of the removal of the N-methyltrityl (Mtt) group during the synthesis of branched peptides. J Pept Res 60:300-303.
    • (2002) J Pept Res , vol.60 , pp. 300-303
    • Li, D.1    Elbert, D.L.2
  • 24
    • 0027236844 scopus 로고
    • Molecular basis of the little mouse phenotype and implications for cell type-specific growth
    • Lin SC, Lin CR, Gukovsky I, Lusis AJ, Sawchenko PE, and Rosenfeld MG (1993) Molecular basis of the little mouse phenotype and implications for cell type-specific growth. Nature (Lond) 364:208-213.
    • (1993) Nature (Lond) , vol.364 , pp. 208-213
    • Lin, S.C.1    Lin, C.R.2    Gukovsky, I.3    Lusis, A.J.4    Sawchenko, P.E.5    Rosenfeld, M.G.6
  • 25
    • 16844366813 scopus 로고    scopus 로고
    • Paired cysteine mutagenesis to establish the pattern of disulfide bonds in the functional intact secretin receptor
    • Lisenbee CS, Dong M, and Miller LJ (2005) Paired cysteine mutagenesis to establish the pattern of disulfide bonds in the functional intact secretin receptor. J Biol Chem 280:12330-12338.
    • (2005) J Biol Chem , vol.280 , pp. 12330-12338
    • Lisenbee, C.S.1    Dong, M.2    Miller, L.J.3
  • 28
    • 0023645714 scopus 로고
    • Analysis of the carbohydrate composition of the pancreatic plasmalemmal glycoprotein affinity labeled by short probes for the cholecystokinin receptor
    • Pearson RK, Miller LJ, Hadac EM, and Powers SP (1987) Analysis of the carbohydrate composition of the pancreatic plasmalemmal glycoprotein affinity labeled by short probes for the cholecystokinin receptor. J Biol Chem 262:13850-13856.
    • (1987) J Biol Chem , vol.262 , pp. 13850-13856
    • Pearson, R.K.1    Miller, L.J.2    Hadac, E.M.3    Powers, S.P.4
  • 29
    • 1342282976 scopus 로고    scopus 로고
    • Spatial proximity between a photolabile residue in position 19 of salmon calcitonin and the amino terminus of the human calcitonin receptor
    • Pham V, Wade JD, Purdue BW, and Sexton PM (2004) Spatial proximity between a photolabile residue in position 19 of salmon calcitonin and the amino terminus of the human calcitonin receptor. J Biol Chem 279:6720-6729.
    • (2004) J Biol Chem , vol.279 , pp. 6720-6729
    • Pham, V.1    Wade, J.D.2    Purdue, B.W.3    Sexton, P.M.4
  • 30
    • 0024009303 scopus 로고
    • Use of N,O-bis-Fmoc-D-Tyr-ONSu for introduction of an oxidative iodination site into cholecystokinin family peptides
    • Powers SP, Pinon DI, and Miller LJ (1988) Use of N,O-bis-Fmoc-D-Tyr-ONSu for introduction of an oxidative iodination site into cholecystokinin family peptides. Int J Pept Protein Res 31:429-434.
    • (1988) Int J Pept Protein Res , vol.31 , pp. 429-434
    • Powers, S.P.1    Pinon, D.I.2    Miller, L.J.3
  • 31
    • 0029898348 scopus 로고    scopus 로고
    • Is there a 'lock' for all agonist 'keys' in 7TM receptors?
    • Schwartz TW and Rosenkilde MM (1996) Is there a 'lock' for all agonist 'keys' in 7TM receptors? Trends Pharmacol Sci 17:213-216.
    • (1996) Trends Pharmacol Sci , vol.17 , pp. 213-216
    • Schwartz, T.W.1    Rosenkilde, M.M.2
  • 32
    • 0031936197 scopus 로고    scopus 로고
    • Secretin and vasoactive intestinal peptide receptors: Members of a unique family of G protein-coupled receptors
    • Ulrich CD 2nd, Holtmann M, and Miller LJ (1998) Secretin and vasoactive intestinal peptide receptors: members of a unique family of G protein-coupled receptors. Gastroenterology 114:382-397.
    • (1998) Gastroenterology , vol.114 , pp. 382-397
    • Ulrich II, C.D.1    Holtmann, M.2    Miller, L.J.3
  • 34
    • 1542316313 scopus 로고    scopus 로고
    • A molecular dissection of the glycoprotein hormone receptors
    • Vassart G, Pardo L, and Costagliola S (2004) A molecular dissection of the glycoprotein hormone receptors. Trends Biochem Sci 29:119-126.
    • (2004) Trends Biochem Sci , vol.29 , pp. 119-126
    • Vassart, G.1    Pardo, L.2    Costagliola, S.3
  • 35
    • 0038745566 scopus 로고    scopus 로고
    • Spatial approximation between a photolabile residue in position 13 of secretin and the amino terminus of the secretin receptor
    • Zang M, Dong M, Pinon DI, Ding XQ, Hadac EM, Li Z, Lybrand TP, and Miller LJ (2003) Spatial approximation between a photolabile residue in position 13 of secretin and the amino terminus of the secretin receptor. Mol Pharmacol 63:993-1001.
    • (2003) Mol Pharmacol , vol.63 , pp. 993-1001
    • Zang, M.1    Dong, M.2    Pinon, D.I.3    Ding, X.Q.4    Hadac, E.M.5    Li, Z.6    Lybrand, T.P.7    Miller, L.J.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.