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Volumn 19, Issue 7, 2005, Pages 1821-1836

Insights into the structure and molecular basis of ligand docking to the G protein-coupled secretin receptor using charge-modified amino-terminal agonist probes

Author keywords

[No Author keywords available]

Indexed keywords

G PROTEIN COUPLED RECEPTOR; SECRETIN;

EID: 22444436330     PISSN: 08888809     EISSN: None     Source Type: Journal    
DOI: 10.1210/me.2004-0421     Document Type: Article
Times cited : (13)

References (43)
  • 1
    • 0031936197 scopus 로고    scopus 로고
    • Secretin and vasoactive intestinal peptide receptors: Members of a unique family of G protein-coupled receptors
    • Ulrich II CD, Holtmann M, 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
  • 2
    • 0029043789 scopus 로고
    • Critical contributions of amino-terminal extracellular domains in agonist binding and activation of secretin and vasoactive intestinal polypeptide receptors. Studies of chimeric receptors
    • Holtmann MH, Hadac EM, Miller LJ 1995 Critical contributions of amino-terminal 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
  • 3
    • 0030801196 scopus 로고    scopus 로고
    • The C-terminal part of VIP is important for receptor binding and activation, as evidenced by chimeric constructs of VIP/secretin
    • Wulff B, Moller Knudsen S, Adelhorst K, Fahrenkrug J 1997 The C-terminal part of VIP is important for receptor binding and activation, as evidenced by chimeric constructs of VIP/secretin. FEBS Lett 413:405-408
    • (1997) FEBS Lett , vol.413 , pp. 405-408
    • Wulff, B.1    Moller Knudsen, S.2    Adelhorst, K.3    Fahrenkrug, J.4
  • 4
    • 0036379869 scopus 로고    scopus 로고
    • Molecular pharmacology of the secretin receptor
    • Dong M, Miller LJ 2002 Molecular pharmacology of the secretin receptor. Receptors Channels 8:189-200
    • (2002) Receptors Channels , vol.8 , pp. 189-200
    • Dong, M.1    Miller, L.J.2
  • 5
    • 0029016549 scopus 로고
    • Properties of chimeric secretin and VIP receptor proteins indicate the importance of the N-terminal domain for ligand discrimination
    • Vilardaga JP, De Neef P, Di Paolo E, Bollen A, Waelbroeck M, Robberecht P 1995 Properties of chimeric secretin and VIP receptor proteins indicate the importance of the N-terminal domain for ligand discrimination. Biochem Biophys Res Commun 211:885-891
    • (1995) Biochem Biophys Res Commun , vol.211 , pp. 885-891
    • Vilardaga, J.P.1    De Neef, P.2    Di Paolo, E.3    Bollen, A.4    Waelbroeck, M.5    Robberecht, P.6
  • 7
    • 0029146992 scopus 로고
    • The amino-terminal fragment of the adenylate cyclase activating polypeptide (PACAP) receptor functions as a high affinity PACAP binding domain
    • Cao YJ, Gimpl G, Fahrenholz F 1995 The amino-terminal fragment of the adenylate cyclase activating polypeptide (PACAP) receptor functions as a high affinity PACAP binding domain. Biochem Biophys Res Commun 212: 673-680
    • (1995) Biochem Biophys Res Commun , vol.212 , pp. 673-680
    • Cao, Y.J.1    Gimpl, G.2    Fahrenholz, F.3
  • 9
    • 0036381416 scopus 로고    scopus 로고
    • Parathyroid hormone 1 receptor: Insights into structure and function
    • Chorev M 2002 Parathyroid hormone 1 receptor: insights into structure and function. Receptors Channels 8:219-242
    • (2002) Receptors Channels , vol.8 , pp. 219-242
    • Chorev, M.1
  • 12
    • 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, 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
  • 14
    • 0034254482 scopus 로고    scopus 로고
    • The N-terminal fragment of human parathyroid hormone receptor 1 constitutes a hormone binding domain and reveals a distinct disulfide pattern
    • Grauschopf U, Lilie H, Honold K, Wozny M, Reusch D, Esswein A, Schafer W, Rucknagel KP, Rudolph R 2000 The N-terminal fragment of human parathyroid hormone receptor 1 constitutes a hormone binding domain and reveals a distinct disulfide pattern. Biochemistry 39:8878-8887
    • (2000) Biochemistry , vol.39 , pp. 8878-8887
    • Grauschopf, U.1    Lilie, H.2    Honold, K.3    Wozny, M.4    Reusch, D.5    Esswein, A.6    Schafer, W.7    Rucknagel, K.P.8    Rudolph, R.9
  • 16
    • 0030820210 scopus 로고    scopus 로고
    • Extracellular cysteines of the corticotropin-releasing factor receptor are critical for ligand interaction
    • Qi LJ, Leung AT, Xiong Y, Marx KA, Abou-Samra AB 1997 Extracellular cysteines of the corticotropin-releasing factor receptor are critical for ligand interaction. Biochemistry 36:12442-12448
    • (1997) Biochemistry , vol.36 , pp. 12442-12448
    • Qi, L.J.1    Leung, A.T.2    Xiong, Y.3    Marx, K.A.4    Abou-Samra, A.B.5
  • 17
    • 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, Miller LJ 1999 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
  • 18
    • 0033534683 scopus 로고    scopus 로고
    • Demonstration of a direct interaction between residue 22 in the carboxyl-terminal half of secretin and the aminoterminal tail of the secretin receptor using photoaffinity labeling
    • Dong M, Wang Y, Pinon DI, Hadac EM, Miller LJ 1999 Demonstration of a direct interaction between residue 22 in the carboxyl-terminal half of secretin and the aminoterminal 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
  • 19
    • 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, 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
  • 20
    • 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, 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
  • 21
    • 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, 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
  • 22
    • 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, 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
  • 23
    • 0141592438 scopus 로고    scopus 로고
    • Photoaffinity labeling demonstrates physical contact between vasoactive intestinal peptide and the Nterminal ectodomain of the human VPAC1 receptor
    • Tan YV, Couvineau A, Van Rampelbergh J, Laburthe M 2003 Photoaffinity labeling demonstrates physical contact between vasoactive intestinal peptide and the Nterminal ectodomain of the human VPAC1 receptor. J Biol Chem 278:36531-36536
    • (2003) J Biol Chem , vol.278 , pp. 36531-36536
    • Tan, Y.V.1    Couvineau, A.2    Van Rampelbergh, J.3    Laburthe, M.4
  • 24
    • 4644228099 scopus 로고    scopus 로고
    • Diffuse pharmacophoric domains of vasoactive intestinal peptide (VIP) and further insights into the interaction of VIP with the N-terminal ectodomain of human VPAC1 receptor by photoaffinity labeling with [Bpa6]-VIP
    • Tan YV, Couvineau A, Laburthe M 2004 Diffuse pharmacophoric domains of vasoactive intestinal peptide (VIP) and further insights into the interaction of VIP with the N-terminal ectodomain of human VPAC1 receptor by photoaffinity labeling with [Bpa6]-VIP. J Biol Chem 279:38889-38894
    • (2004) J Biol Chem , vol.279 , pp. 38889-38894
    • Tan, Y.V.1    Couvineau, A.2    Laburthe, M.3
  • 25
    • 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, Miller LJ 2004 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
  • 26
    • 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, Miller LJ 2004 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
  • 27
    • 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, 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
  • 28
    • 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, Miller LJ 2004 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
  • 29
    • 0024466067 scopus 로고
    • Chemical properties of the histidine residue of secretin: Evidence for a specific intramolecular interaction
    • Hefford MA, Kaplan H 1989 Chemical properties of the histidine residue of secretin: evidence for a specific intramolecular interaction. Biochim Biophys Acta 998: 267-270
    • (1989) Biochim Biophys Acta , vol.998 , pp. 267-270
    • Hefford, M.A.1    Kaplan, H.2
  • 30
    • 0029790078 scopus 로고    scopus 로고
    • Role of receptor phosphorylation in desensitization and internalization of the secretin receptor
    • Holtmann MH, Roettger BF, Pinon DI, Miller LJ 1996 Role of receptor phosphorylation in desensitization and internalization of the secretin receptor. J Biol Chem 271:23566-23571
    • (1996) J Biol Chem , vol.271 , pp. 23566-23571
    • Holtmann, M.H.1    Roettger, B.F.2    Pinon, D.I.3    Miller, L.J.4
  • 31
    • 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, 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
  • 32
    • 0034614619 scopus 로고    scopus 로고
    • Photoaffinity cross-linking identifies differences in the interactions of an agonist and an antagonist with the parathyroid hormone/parathyroid hormone-related protein receptor
    • Behar V, Bisello A, Bitan G, Rosenblatt M, Chorev M 2000 Photoaffinity cross-linking identifies differences in the interactions of an agonist and an antagonist with the parathyroid hormone/parathyroid hormone-related protein receptor. J Biol Chem 275:9-17
    • (2000) J Biol Chem , vol.275 , pp. 9-17
    • Behar, V.1    Bisello, A.2    Bitan, G.3    Rosenblatt, M.4    Chorev, M.5
  • 34
    • 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, 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
  • 35
    • 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, 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
  • 36
    • 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, 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
  • 37
    • 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, 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
  • 39
    • 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, 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
  • 40
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK 1970 Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 41
    • 0032557448 scopus 로고    scopus 로고
    • Direct identification of a second distinct site of contact between cholecystokinin and its receptor
    • Hadac EM, Pinon DI, Ji Z, Holicky EL, Henne RM, Lybrand TP, Miller LJ 1998 Direct identification of a second distinct site of contact between cholecystokinin and its receptor. J Biol Chem 273:12988-12993
    • (1998) J Biol Chem , vol.273 , pp. 12988-12993
    • Hadac, E.M.1    Pinon, D.I.2    Ji, Z.3    Holicky, E.L.4    Henne, R.M.5    Lybrand, T.P.6    Miller, L.J.7
  • 43
    • 0019061918 scopus 로고
    • Ligand: A versatile computerized approach for characterization of ligand-binding systems
    • Munson PJ, Rodbard D 1980 Ligand: a versatile computerized approach for characterization of ligand-binding systems. Anal Biochem 107:220-239
    • (1980) Anal Biochem , vol.107 , pp. 220-239
    • Munson, P.J.1    Rodbard, D.2


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