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Volumn 26, Issue 12, 2012, Pages 5092-5105

Mapping spatial approximations between the amino terminus of secretin and each of the extracellular loops of its receptor using cysteine trapping

Author keywords

Class B GPCRs; Ligand binding; Molecular modeling

Indexed keywords

CYSTEINE; SECRETIN;

EID: 84870352082     PISSN: None     EISSN: 15306860     Source Type: Journal    
DOI: 10.1096/fj.12-212399     Document Type: Article
Times cited : (33)

References (41)
  • 2
    • 84860513814 scopus 로고    scopus 로고
    • Structure-based drug screening for G-protein-coupled receptors
    • Shoichet, B. K., and Kobilka, B. K. (2012) Structure-based drug screening for G-protein-coupled receptors. Trends Pharmacol. Sci. 33, 268-272
    • (2012) Trends Pharmacol. Sci. , vol.33 , pp. 268-272
    • Shoichet, B.K.1    Kobilka, B.K.2
  • 3
    • 79959872463 scopus 로고    scopus 로고
    • Molecular basis of secretin docking to its intact receptor using multiple photolabile probes distributed throughout the pharmacophore
    • Dong, M., Lam, P. C., Pinon, D. I., Hosohata, K., Orry, A., Sexton, P. M., Abagyan, R., and Miller, L. J. (2011) Molecular basis of secretin docking to its intact receptor using multiple photolabile probes distributed throughout the pharmacophore. J. Biol. Chem. 286, 23888-23899
    • (2011) J. Biol. Chem. , vol.286 , pp. 23888-23899
    • Dong, M.1    Lam, P.C.2    Pinon, D.I.3    Hosohata, K.4    Orry, A.5    Sexton, P.M.6    Abagyan, R.7    Miller, L.J.8
  • 4
    • 67149136711 scopus 로고    scopus 로고
    • Passing the baton in class B GPCRs: Peptide hormone activation via helix induction?
    • Parthier, C., Reedtz-Runge, S., Rudolph, R., and Stubbs, M. T. (2009) Passing the baton in class B GPCRs: peptide hormone activation via helix induction? Trends Biochem. Sci. 34, 303-310
    • (2009) Trends Biochem. Sci. , vol.34 , pp. 303-310
    • Parthier, C.1    Reedtz-Runge, S.2    Rudolph, R.3    Stubbs, M.T.4
  • 5
    • 77955302857 scopus 로고    scopus 로고
    • Spatial approximations between residues 6 and 12 in the amino-terminal region of glucagon-like peptide 1 and its receptor: A region critical for biological activity
    • Chen, Q., Pinon, D. I., Miller, L. J., and Dong, M. (2010) Spatial approximations between residues 6 and 12 in the amino-terminal region of glucagon-like peptide 1 and its receptor: a region critical for biological activity. J. Biol. Chem. 285, 24508-24518
    • (2010) J. Biol. Chem. , vol.285 , pp. 24508-24518
    • Chen, Q.1    Pinon, D.I.2    Miller, L.J.3    Dong, M.4
  • 6
    • 47949116776 scopus 로고    scopus 로고
    • Spatial approximation between secretin residue five and the third extracellular loop of its receptor provides new insight into the molecular basis of natural agonist binding
    • Dong, M., Lam, P. C., Pinon, D. I., Sexton, P. M., Abagyan, R., and Miller, L. J. (2008) Spatial approximation between secretin residue five and the third extracellular loop of its receptor provides new insight into the molecular basis of natural agonist binding. Mol. Pharmacol. 74, 413-422
    • (2008) Mol. Pharmacol. , vol.74 , pp. 413-422
    • Dong, M.1    Lam, P.C.2    Pinon, D.I.3    Sexton, P.M.4    Abagyan, R.5    Miller, L.J.6
  • 7
    • 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
    • DOI 10.1074/jbc.M310407200
    • Dong, M., Li, Z., Pinon, D. I., Lybrand, T. P., and Miller, L. J. (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 (Pubitemid 38114281)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.4 , pp. 2894-2903
    • Dong, M.1    Li, Z.2    Pinon, D.I.3    Lybrand, T.P.4    Miller, L.J.5
  • 8
    • 14244265111 scopus 로고    scopus 로고
    • Site-specific disulfide capture of agonist and antagonist peptides on the C5a receptor
    • DOI 10.1074/jbc.C400500200
    • Buck, E., Bourne, H., and Wells, J. A. (2005) Site-specific disulfide capture of agonist and antagonist peptides on the C5a receptor. J. Biol. Chem. 280, 4009-4012 (Pubitemid 40288561)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.6 , pp. 4009-4012
    • Buck, E.1    Bourne, H.2    Wells, J.A.3
  • 10
    • 43149124854 scopus 로고    scopus 로고
    • Structure of the complement factor 5a receptor-ligand complex studied by disulfide trapping and molecular modeling
    • Hagemann, I. S., Miller, D. L., Klco, J. M., Nikiforovich, G. V., and Baranski, T. J. (2008) Structure of the complement factor 5a receptor-ligand complex studied by disulfide trapping and molecular modeling. J. Biol. Chem. 283, 7763-7775
    • (2008) J. Biol. Chem. , vol.283 , pp. 7763-7775
    • Hagemann, I.S.1    Miller, D.L.2    Klco, J.M.3    Nikiforovich, G.V.4    Baranski, T.J.5
  • 11
    • 44449177208 scopus 로고    scopus 로고
    • Mapping peptide hormone-receptor interactions using a disulfide-trapping approach
    • DOI 10.1021/bi800122f
    • Monaghan, P., Thomas, B. E., Woznica, I., Wittelsberger, A., Mierke, D. F., and Rosenblatt, M. (2008) Mapping peptide hormone-receptor interactions using a disulfide-trapping approach. Biochemistry 47, 5889-5895 (Pubitemid 351770019)
    • (2008) Biochemistry , vol.47 , Issue.22 , pp. 5889-5895
    • Monaghan, P.1    Thomas, B.E.2    Woznica, I.3    Wittelsberger, A.4    Mierke, D.F.5    Rosenblatt, M.6
  • 13
    • 0017647288 scopus 로고
    • Interaction of synthetic 10 tyrosyl analogues of secretin with hormone receptors on pancreatic acinar cells
    • Gardner, J. D., Conlon, T. P., Beyerman, H. C., and Van Zon, A. (1977) Interaction of synthetic 10-tyrosyl analogues of secretin with hormone receptors on pancreatic acinar cells. Gastroenterology 73, 52-56 (Pubitemid 8143340)
    • (1977) Gastroenterology , vol.73 , Issue.1 , pp. 52-56
    • Gardner, J.D.1    Conlon, T.P.2    Beyerman, H.C.3    Van Zon, A.4
  • 14
    • 0024009303 scopus 로고
    • Use of N,O-bis-Fmoc-D-Tyr-ONSu for introduction of an oxidative iodination site into cholecystokinin family peptides
    • Powers, S. P., Pinon, D. I., and Miller, L. J. (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
  • 15
    • 35649028687 scopus 로고    scopus 로고
    • Transmembrane segment IV contributes a functionally important interface for oligomerization of the class II G protein-coupled secretin receptor
    • DOI 10.1074/jbc.M702325200
    • Harikumar, K. G., Pinon, D. I., and Miller, L. J. (2007) Transmembrane segment IV contributes a functionally important interface for oligomerization of the class II G protein-coupled secretin receptor. J. Biol. Chem. 282, 30363-30372 (Pubitemid 350035177)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.42 , pp. 30363-30372
    • Harikumar, K.G.1    Pinon, D.I.2    Miller, L.J.3
  • 16
    • 0021770787 scopus 로고
    • High level transient expression of a chloramphenicol acetyl transferase gene by DEAE-dextran mediated DNA transfection coupled with a dimethyl sulfoxide or glycerol shock treatment
    • Lopata, M. A., Cleveland, D. W., and Sollner-Webb, B. (1984) High level transient expression of a chloramphenicol acetyl transferase gene by DEAE-dextran mediated DNA transfection coupled with a dimethyl sulfoxide or glycerol shock treatment. Nucleic Acids Res. 12, 5707-5717
    • (1984) Nucleic Acids Res. , vol.12 , pp. 5707-5717
    • Lopata, M.A.1    Cleveland, D.W.2    Sollner-Webb, B.3
  • 17
    • 0019061918 scopus 로고
    • Ligand: A versatile computerized approach for characterization of ligand-binding systems
    • Munson, P. J., and 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
  • 18
    • 84859773823 scopus 로고    scopus 로고
    • Differential determinants for coupling of distinct G proteins with the class B secretin receptor
    • Garcia, G. L., Dong, M., and Miller, L. J. (2012) Differential determinants for coupling of distinct G proteins with the class B secretin receptor. Am. J. Physiol. Cell Phys. 302, C1202-1212
    • (2012) Am. J. Physiol. Cell Phys. , vol.302
    • Garcia, G.L.1    Dong, M.2    Miller, L.J.3
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (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
  • 20
    • 84986522918 scopus 로고
    • Icm - A new method for protein modeling and design - applications to docking and structure prediction from the distorted native confirmation
    • Abagyan, R., Totrov, M., and Kuznetsov, D. (1994) Icm - a new method for protein modeling and design - applications to docking and structure prediction from the distorted native confirmation. J. Comput. Chem. 15, 488-506
    • (1994) J. Comput. Chem. , vol.15 , pp. 488-506
    • Abagyan, R.1    Totrov, M.2    Kuznetsov, D.3
  • 22
    • 36349035022 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer analysis of secretin docking to its receptor: Mapping distances between residues distributed throughout the ligand pharmacophore and distinct receptor residues
    • DOI 10.1074/jbc.M704563200
    • Harikumar, K. G., Lam, P. C., Dong, M., Sexton, P. M., Abagyan, R., and Miller, L. J. (2007) Fluorescence resonance energy transfer analysis of secretin docking to its receptor: mapping distances between residues distributed throughout the ligand pharmacophore and distinct receptor residues. J. Biol. Chem. 282, 32834-32843 (Pubitemid 350159279)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.45 , pp. 32834-32843
    • Harikumar, K.G.1    Lam, P.C.-H.2    Dong, M.3    Sexton, P.M.4    Abagyan, R.5    Miller, L.J.6
  • 25
    • 79953688273 scopus 로고    scopus 로고
    • Importance of each residue within secretin for receptor binding and biological activity
    • Dong, M., Le, A., Te, J. A., Pinon, D. I., Bordner, A. J., and Miller, L. J. (2011) Importance of each residue within secretin for receptor binding and biological activity. Biochemistry 50, 2983-2993
    • (2011) Biochemistry , vol.50 , pp. 2983-2993
    • Dong, M.1    Le, A.2    Te, J.A.3    Pinon, D.I.4    Bordner, A.J.5    Miller, L.J.6
  • 26
    • 15844385219 scopus 로고    scopus 로고
    • Multiple extracellular loop domains contribute critical determinants for agonist binding and activation of the secretin receptor
    • DOI 10.1074/jbc.271.25.14944
    • Holtmann, M. H., Ganguli, S., Hadac, E. M., Dolu, V., and Miller, L. J. (1996) Multiple extracellular loop domains contribute critical determinants for agonist binding and activation of the secretin receptor. J. Biol. Chem. 271, 14944-14949 (Pubitemid 26197574)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.25 , pp. 14944-14949
    • Holtmann, M.H.1    Ganguli, S.2    Hadac, E.M.3    Dolu, V.4    Miller, L.J.5
  • 28
    • 0032513222 scopus 로고    scopus 로고
    • Contribution of the second transmembrane helix of the secretin receptor to the positioning of secretin
    • DOI 10.1016/S0014-5793(98)00175-6, PII S0014579398001756
    • Di Paolo, E., De Neef, P., Moguilevsky, N., Petry, H., Bollen, A., Waelbroeck, M., and Robberecht, P. (1998) Contribution of the second transmembrane helix of the secretin receptor to the positioning of secretin. FEBS Lett. 424, 207-210 (Pubitemid 28135315)
    • (1998) FEBS Letters , vol.424 , Issue.3 , pp. 207-210
    • Di, P.E.1    De Neef, P.2    Moguilevsky, N.3    Petry, H.4    Bollen, A.5    Waelbroeck, M.6    Robberecht, P.7
  • 29
    • 0032770346 scopus 로고    scopus 로고
    • Mutations of aromatic residues in the first transmembrane helix impair signalling by the secretin receptor
    • Di Paolo, E., Petry, H., Moguilevsky, N., Bollen, A., De Neef, P., Waelbroeck, M., and Robberecht, P. (1999) Mutations of aromatic residues in the first transmembrane helix impair signalling by the secretin receptor. Receptors Channels 6, 309-315 (Pubitemid 29329025)
    • (1999) Receptors and Channels , vol.6 , Issue.4 , pp. 309-315
    • Di, P.E.1    Petry, H.2    Moguilevsky, N.3    Bollen, A.4    De Neef, P.5    Waelbroeck, M.6    Robberecht, P.7
  • 30
    • 15844371700 scopus 로고    scopus 로고
    • Transmembrane residues of the parathyroid hormone (PTH)/PTH-related peptide receptor that specifically affect binding and signaling by agonist ligands
    • DOI 10.1074/jbc.271.22.12820
    • Gardella, T. J., Luck, M. D., Fan, M. H., and Lee, C. (1996) Transmembrane residues of the parathyroid hormone (PTH)/PTH-related peptide receptor that specifically affect binding and signaling by agonist ligands. J. Biol. Chem. 271, 12820-12825 (Pubitemid 26175855)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.22 , pp. 12820-12825
    • Gardella, T.J.1    Luck, M.D.2    Fan, M.-H.3    Lee, C.4
  • 31
    • 0041344589 scopus 로고    scopus 로고
    • Three distinct epitopes on the extracellular face of the glucagon receptor determine specificity for the glucagon amino terminus
    • DOI 10.1074/jbc.M301085200
    • Runge, S., Gram, C., Brauner-Osborne, H., Madsen, K., Knudsen, L. B., and Wulff, B. S. (2003) Three distinct epitopes on the extracellular face of the glucagon receptor determine specificity for the glucagon amino terminus. J. Biol. Chem. 278, 28005-28010 (Pubitemid 36899996)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.30 , pp. 28005-28010
    • Runge, S.1    Gram, C.2    Brauner-Osborne, H.3    Madsen, K.4    Knudsen, L.B.5    Wulff, B.S.6
  • 32
    • 0035846913 scopus 로고    scopus 로고
    • 1 receptor second transmembrane helix are essential for ligand binding and signal transduction
    • DOI 10.1074/jbc.M007686200
    • Solano, R. M., Langer, I., Perret, J., Vertongen, P., Juarranz, M. G., Robberecht, P., and Waelbroeck, M. (2001) Two basic residues of the h-VPAC1 receptor second transmembrane helix are essential for ligand binding and signal transduction. J. Biol. Chem. 276, 1084-1088 (Pubitemid 32098012)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.2 , pp. 1084-1088
    • Solano, R.M.1    Langer, I.2    Perret, J.3    Vertongen, P.4    Juarranz, M.G.5    Robberecht, P.6    Waelbroeck, M.7
  • 33
    • 0034870577 scopus 로고    scopus 로고
    • 2: Role of basic residues in the second transmembrane helix
    • Vertongen, P., Solano, R. M., Perret, J., Langer, I., Robberecht, P., and Waelbroeck, M. (2001) Mutational analysis of the human vasoactive intestinal peptide receptor subtype VPAC(2): role of basic residues in the second transmembrane helix. Br. J. Pharmacol. 133, 1249-1254 (Pubitemid 32783485)
    • (2001) British Journal of Pharmacology , vol.133 , Issue.8 , pp. 1249-1254
    • Vertongen, P.1    Solano, R.M.2    Perret, J.3    Langer, I.4    Robberecht, P.5    Waelbroeck, M.6
  • 34
    • 28244464442 scopus 로고    scopus 로고
    • Photoaffinity cross-linking of the corticotropin-releasing factor receptor type 1 with photoreactive urocortin analogues
    • DOI 10.1021/bi0507027
    • Kraetke, O., Holeran, B., Berger, H., Escher, E., Bienert, M., and Beyermann, M. (2005) Photoaffinity cross-linking of the corticotropin-releasing factor receptor type 1 with photoreactive urocortin analogues. Biochemistry 44, 15569-15577 (Pubitemid 41706141)
    • (2005) Biochemistry , vol.44 , Issue.47 , pp. 15569-15577
    • Kraetke, O.1    Holeran, B.2    Berger, H.3    Escher, E.4    Bienert, M.5    Beyermann, M.6
  • 35
    • 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
    • DOI 10.1074/jbc.275.1.9
    • Behar, V., Bisello, A., Bitan, G., Rosenblatt, M., and 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 (Pubitemid 30038946)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.1 , pp. 9-17
    • Behar, V.1    Bisello, A.2    Bitan, G.3    Rosenblatt, M.4    Chorev, M.5
  • 36
    • 0035900738 scopus 로고    scopus 로고
    • Identification of determinants of inverse agonism in a constitutively active parathyroid hormone/parathyroid hormone-related peptide receptor by photoaffinity cross-linking and mutational analysis
    • Gensure, R. C., Carter, P. H., Petroni, B. D., Juppner, H., and Gardella, T. J. (2001) Identification of determinants of inverse agonism in a constitutively active parathyroid hormone/parathyroid hormone-related peptide receptor by photoaffinity cross-linking and mutational analysis. J. Biol. Chem. 276, 42692-42699
    • (2001) J. Biol. Chem. , vol.276 , pp. 42692-42699
    • Gensure, R.C.1    Carter, P.H.2    Petroni, B.D.3    Juppner, H.4    Gardella, T.J.5
  • 37
    • 33748282179 scopus 로고    scopus 로고
    • Multi-template approach to modeling engineered disulfide bonds
    • Pellequer, J. L., and Chen, S. W. (2006) Multi-template approach to modeling engineered disulfide bonds. Proteins 65, 192-202
    • (2006) Proteins , vol.65 , pp. 192-202
    • Pellequer, J.L.1    Chen, S.W.2
  • 38
    • 0028910510 scopus 로고
    • Molecular cloning and functional expression of a human pancreatic secretin receptor
    • Jiang, S., and Ulrich, C. (1995) Molecular cloning and functional expression of a human pancreatic secretin receptor. Biochem. Biophys. Res. Commun. 207, 883-890
    • (1995) Biochem. Biophys. Res. Commun. , vol.207 , pp. 883-890
    • Jiang, S.1    Ulrich, C.2
  • 39
    • 34548476934 scopus 로고    scopus 로고
    • Critical role for the second extracellular loop in the binding of both orthosteric and allosteric G protein-coupled receptor ligands
    • DOI 10.1074/jbc.M702311200
    • Avlani, V. A., Gregory, K. J., Morton, C. J., Parker, M. W., Sexton, P. M., and Christopoulos, A. (2007) Critical role for the second extracellular loop in the binding of both orthosteric and allosteric G protein-coupled receptor ligands. J. Biol. Chem. 282, 25677-25686 (Pubitemid 47372845)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.35 , pp. 25677-25686
    • Avlani, V.A.1    Gregory, K.J.2    Morton, C.J.3    Parker, M.W.4    Sexton, P.M.5    Christopoulos, A.6


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