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Volumn 31, Issue 1, 2010, Pages 170-176

Mapping interaction sites within the N-terminus of the calcitonin gene-related peptide receptor; the role of residues 23-60 of the calcitonin receptor-like receptor

Author keywords

Alanine scan; CGRP; CLR; Family B GPCRs; Molecular modelling; RAMP1

Indexed keywords

ALANINE; CALCITONIN GENE RELATED PEPTIDE RECEPTOR; CALCITONIN RECEPTOR LIKE RECEPTOR; CYCLIC AMP; CYSTEINE; GLUTAMINE; GLYCINE; ISOLEUCINE; LEUCINE; RECEPTOR ACTIVITY MODIFYING PROTEIN 1; THREONINE; TYROSINE;

EID: 72749105799     PISSN: 01969781     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.peptides.2009.10.021     Document Type: Article
Times cited : (23)

References (29)
  • 1
  • 2
    • 33746747483 scopus 로고    scopus 로고
    • Identification of specific calcitonin-like receptor residues important for calcitonin gene-related peptide high affinity binding
    • Banerjee S., Evanson J., Harris E., Lowe S.L., Thomasson K.A., and Porter J.E. Identification of specific calcitonin-like receptor residues important for calcitonin gene-related peptide high affinity binding. BMC Pharmacol 6 (2006) 9
    • (2006) BMC Pharmacol , vol.6 , pp. 9
    • Banerjee, S.1    Evanson, J.2    Harris, E.3    Lowe, S.L.4    Thomasson, K.A.5    Porter, J.E.6
  • 4
    • 0033039911 scopus 로고    scopus 로고
    • Multiple amylin receptors arise from receptor activity-modifying protein interaction with the calcitonin receptor gene product
    • Christopoulos G., Perry K.J., Morfis M., Tilakaratne N., Gao Y., Fraser N.J., et al. Multiple amylin receptors arise from receptor activity-modifying protein interaction with the calcitonin receptor gene product. Mol Pharmacol 56 (1999) 235-242
    • (1999) Mol Pharmacol , vol.56 , pp. 235-242
    • Christopoulos, G.1    Perry, K.J.2    Morfis, M.3    Tilakaratne, N.4    Gao, Y.5    Fraser, N.J.6
  • 6
    • 11244331476 scopus 로고    scopus 로고
    • A key role for transmembrane prolines in calcitonin receptor-like receptor agonist binding and signalling: implications for family B G-protein-coupled receptors
    • Conner A.C., Hay D.L., Simms J., Howitt S.G., Schindler M., Smith D.M., et al. A key role for transmembrane prolines in calcitonin receptor-like receptor agonist binding and signalling: implications for family B G-protein-coupled receptors. Mol Pharmacol 67 (2005) 20-31
    • (2005) Mol Pharmacol , vol.67 , pp. 20-31
    • Conner, A.C.1    Hay, D.L.2    Simms, J.3    Howitt, S.G.4    Schindler, M.5    Smith, D.M.6
  • 7
    • 49449095044 scopus 로고    scopus 로고
    • Functional and biophysical analysis of the C-terminus of the CGRP-receptor; a family B GPCR
    • Conner M., Hicks M.R., Dafforn T., Knowles T.J., Ludwig C., Staddon S., et al. Functional and biophysical analysis of the C-terminus of the CGRP-receptor; a family B GPCR. Biochemistry 47 (2008) 8434-8444
    • (2008) Biochemistry , vol.47 , pp. 8434-8444
    • Conner, M.1    Hicks, M.R.2    Dafforn, T.3    Knowles, T.J.4    Ludwig, C.5    Staddon, S.6
  • 8
    • 0034613266 scopus 로고    scopus 로고
    • CGRP-RCP, a novel protein required for signal transduction at calcitonin gene-related peptide and adrenomedullin receptors
    • Evans B.N., Rosenblatt M.I., Mnayer L.O., Oliver K.R., and Dickerson I.M. CGRP-RCP, a novel protein required for signal transduction at calcitonin gene-related peptide and adrenomedullin receptors. J Biol Chem 275 (2000) 31438-31443
    • (2000) J Biol Chem , vol.275 , pp. 31438-31443
    • Evans, B.N.1    Rosenblatt, M.I.2    Mnayer, L.O.3    Oliver, K.R.4    Dickerson, I.M.5
  • 9
    • 0347383758 scopus 로고    scopus 로고
    • Modeller: generation and refinement of homology-based protein structure models
    • Academic Press pp. 461-91
    • Fiser A., Sali A., Charles W., and Carter JaRM.S. Modeller: generation and refinement of homology-based protein structure models. Methods in enzymology (2003), Academic Press pp. 461-91
    • (2003) Methods in enzymology
    • Fiser, A.1    Sali, A.2    Charles, W.3    Carter, JaRM.S.4
  • 10
    • 34247561729 scopus 로고    scopus 로고
    • Structure of the N-terminal domain of a type B1 G protein-coupled receptor in complex with a peptide ligand
    • Grace C.R., Perrin M.H., Gulyas J., Digruccio M.R., Cantle J.P., Rivier J.E., et al. Structure of the N-terminal domain of a type B1 G protein-coupled receptor in complex with a peptide ligand. Proc Natl Acad Sci USA 104 (2007) 4858-4863
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 4858-4863
    • Grace, C.R.1    Perrin, M.H.2    Gulyas, J.3    Digruccio, M.R.4    Cantle, J.P.5    Rivier, J.E.6
  • 11
    • 0035826532 scopus 로고    scopus 로고
    • Mutations of the asparagine117 residue of a receptor activity-modifying protein 1-dependent human calcitonin gene-related peptide receptor result in selective loss of function
    • Gujer R., Aldecoa A., Buhlmann N., Leuthauser K., Muff R., Fischer J.A., et al. Mutations of the asparagine117 residue of a receptor activity-modifying protein 1-dependent human calcitonin gene-related peptide receptor result in selective loss of function. Biochemistry 40 (2001) 5392-5398
    • (2001) Biochemistry , vol.40 , pp. 5392-5398
    • Gujer, R.1    Aldecoa, A.2    Buhlmann, N.3    Leuthauser, K.4    Muff, R.5    Fischer, J.A.6
  • 12
    • 35748982441 scopus 로고    scopus 로고
    • Functional calcitonin gene-related peptide receptors are formed by the asymmetric assembly of a calcitonin receptor-like receptor homo-oligomer and a monomer of receptor activity-modifying protein-1
    • Heroux M., Hogue M., Lemieux S., and Bouvier M. Functional calcitonin gene-related peptide receptors are formed by the asymmetric assembly of a calcitonin receptor-like receptor homo-oligomer and a monomer of receptor activity-modifying protein-1. J Biol Chem 282 (2007) 31610-31620
    • (2007) J Biol Chem , vol.282 , pp. 31610-31620
    • Heroux, M.1    Hogue, M.2    Lemieux, S.3    Bouvier, M.4
  • 13
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS, 4 algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • Hess B., Kutzner C., van der Spoel D., and Lindahl E. GROMACS, 4 algorithms for highly efficient, load-balanced, and scalable molecular simulation. J Chem Theory Comput 4 (2008) 435-447
    • (2008) J Chem Theory Comput , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    van der Spoel, D.3    Lindahl, E.4
  • 14
    • 17144382079 scopus 로고    scopus 로고
    • The N-terminal extracellular domain 23-60 of the calcitonin receptor-like receptor in chimeras with the parathyroid hormone receptor mediates association with receptor activity-modifying protein 1
    • Ittner L.M., Koller D., Muff R., Fischer J.A., and Born W. The N-terminal extracellular domain 23-60 of the calcitonin receptor-like receptor in chimeras with the parathyroid hormone receptor mediates association with receptor activity-modifying protein 1. Biochemistry 44 (2005) 5749-5754
    • (2005) Biochemistry , vol.44 , pp. 5749-5754
    • Ittner, L.M.1    Koller, D.2    Muff, R.3    Fischer, J.A.4    Born, W.5
  • 15
    • 0037145808 scopus 로고    scopus 로고
    • The extreme N-terminus of the calcitonin-like receptor contributes to the selective interaction with adrenomedullin or calcitonin gene-related peptide
    • Koller D., Born W., Leuthauser K., Fluhmann B., McKinney R.A., Fischer J.A., et al. The extreme N-terminus of the calcitonin-like receptor contributes to the selective interaction with adrenomedullin or calcitonin gene-related peptide. FEBS Lett 531 (2002) 464-468
    • (2002) FEBS Lett , vol.531 , pp. 464-468
    • Koller, D.1    Born, W.2    Leuthauser, K.3    Fluhmann, B.4    McKinney, R.A.5    Fischer, J.A.6
  • 16
    • 55549092099 scopus 로고    scopus 로고
    • Crystal structure of the human receptor activity-modifying protein 1 extracellular domain
    • Kusano S., Kukimoto-Niino M., Akasaka R., Toyama M., Terada T., Shirouzu M., et al. Crystal structure of the human receptor activity-modifying protein 1 extracellular domain. Protein Sci 17 (2008) 1907-1914
    • (2008) Protein Sci , vol.17 , pp. 1907-1914
    • Kusano, S.1    Kukimoto-Niino, M.2    Akasaka, R.3    Toyama, M.4    Terada, T.5    Shirouzu, M.6
  • 17
    • 0035175679 scopus 로고    scopus 로고
    • PDBsum: summaries and analyses of PDB structures
    • Laskowski R.A. PDBsum: summaries and analyses of PDB structures. Nucleic Acids Res 29 (2001) 221-222
    • (2001) Nucleic Acids Res , vol.29 , pp. 221-222
    • Laskowski, R.A.1
  • 18
    • 16844366813 scopus 로고    scopus 로고
    • Paired cysteine mutagenesis to establish the pattern of disulfide bonds in the functional intact secretin receptor
    • Lisenbee C.S., Dong M., and Miller L.J. Paired cysteine mutagenesis to establish the pattern of disulfide bonds in the functional intact secretin receptor. J Biol Chem 280 (2005) 12330-12338
    • (2005) J Biol Chem , vol.280 , pp. 12330-12338
    • Lisenbee, C.S.1    Dong, M.2    Miller, L.J.3
  • 19
    • 0032574982 scopus 로고    scopus 로고
    • RAMPs regulate the transport and ligand specificity of the calcitonin-receptor-like receptor
    • McLatchie L.M., Fraser N.J., Main M.J., Wise A., Brown J., Thompson N., et al. RAMPs regulate the transport and ligand specificity of the calcitonin-receptor-like receptor. Nature 393 (1998) 333-339
    • (1998) Nature , vol.393 , pp. 333-339
    • McLatchie, L.M.1    Fraser, N.J.2    Main, M.J.3    Wise, A.4    Brown, J.5    Thompson, N.6
  • 20
    • 0033562633 scopus 로고    scopus 로고
    • Use of pair potentials across protein interfaces in screening predicted docked complexes
    • Moont G., Gabb H.A., and Sternberg M.J. Use of pair potentials across protein interfaces in screening predicted docked complexes. Proteins 35 (1999) 364-373
    • (1999) Proteins , vol.35 , pp. 364-373
    • Moont, G.1    Gabb, H.A.2    Sternberg, M.J.3
  • 21
    • 0033278998 scopus 로고    scopus 로고
    • An amylin receptor is revealed following co-transfection of a calcitonin receptor with receptor activity modifying proteins-1 or -3
    • Muff R., Buhlmann N., Fischer J.A., and Born W. An amylin receptor is revealed following co-transfection of a calcitonin receptor with receptor activity modifying proteins-1 or -3. Endocrinology 140 (1999) 2924-2927
    • (1999) Endocrinology , vol.140 , pp. 2924-2927
    • Muff, R.1    Buhlmann, N.2    Fischer, J.A.3    Born, W.4
  • 23
    • 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. Passing the baton in class B GPCRs: peptide hormone activation via helix induction?. Trends Biochem Sci 34 (2009) 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
  • 24
    • 0037375615 scopus 로고    scopus 로고
    • Ab initio construction of polypeptide fragments: accuracy of loop decoy discrimination by an all-atom statistical potential and the AMBER force field with the Generalized Born solvation model
    • de Bakker P.I.W., Depristo M.A., Burke D.F., and Blundell T.L. Ab initio construction of polypeptide fragments: accuracy of loop decoy discrimination by an all-atom statistical potential and the AMBER force field with the Generalized Born solvation model. Proteins: Struct Funct Genet 51 (2003) 21-40
    • (2003) Proteins: Struct Funct Genet , vol.51 , pp. 21-40
    • de Bakker, P.I.W.1    Depristo, M.A.2    Burke, D.F.3    Blundell, T.L.4
  • 25
    • 42449160533 scopus 로고    scopus 로고
    • Molecular recognition of parathyroid hormone by its G protein-coupled receptor
    • Pioszak A.A., and Xu H.E. Molecular recognition of parathyroid hormone by its G protein-coupled receptor. Proc Natl Acad Sci USA 105 (2008) 5034-5039
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 5034-5039
    • Pioszak, A.A.1    Xu, H.E.2
  • 26
    • 4043171970 scopus 로고    scopus 로고
    • The GB/SA continuum model for solvation. A fast analytical method for the calculation of approximate born radii
    • Qiu D., Shenkin P.S., Hollinger F.P., and Still W.C. The GB/SA continuum model for solvation. A fast analytical method for the calculation of approximate born radii. J Phys Chem A 101 (1997) 3005-3014
    • (1997) J Phys Chem A , vol.101 , pp. 3005-3014
    • Qiu, D.1    Shenkin, P.S.2    Hollinger, F.P.3    Still, W.C.4
  • 27
    • 70350434125 scopus 로고    scopus 로고
    • Novel peptide antagonists of adrenomedullin and calcitonin gene-related peptide receptors; identification, pharmacological characterization and interactions with position 74 in RAMP1/3
    • Robinson S.D., Aitken J.F., Bailey R.J., Poyner D.R., and Hay D.L. Novel peptide antagonists of adrenomedullin and calcitonin gene-related peptide receptors; identification, pharmacological characterization and interactions with position 74 in RAMP1/3. J Pharmacol Exp Ther (2009)
    • (2009) J Pharmacol Exp Ther
    • Robinson, S.D.1    Aitken, J.F.2    Bailey, R.J.3    Poyner, D.R.4    Hay, D.L.5
  • 29
    • 46449139781 scopus 로고    scopus 로고
    • Ab initio folding of terminal segments with secondary structures reveals the fine difference between two closely related all-atom statistical energy functions
    • Yuedong Yang Y.Z. Ab initio folding of terminal segments with secondary structures reveals the fine difference between two closely related all-atom statistical energy functions. Protein Sci 17 (2008) 1212-1219
    • (2008) Protein Sci , vol.17 , pp. 1212-1219
    • Yuedong Yang, Y.Z.1


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