메뉴 건너뛰기




Volumn 48, Issue 1, 2009, Pages 198-205

Structure-function analysis of RAMP1 by alanine mutagenesis

Author keywords

[No Author keywords available]

Indexed keywords

CELL SURFACES; INTEGRAL COMPONENTS; LIGAND BINDING; PROTEIN INTERACTIONS; RECEPTOR ACTIVITY; RECEPTOR TRAFFICKING; RECOGNITION SITES; STRUCTURE FUNCTION ANALYSIS;

EID: 58549084401     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi801869n     Document Type: Article
Times cited : (26)

References (22)
  • 2
    • 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. (1999) An amylin receptor is revealed following co -transfection of a calcitonin receptor with receptor activity modifying proteins-1 or -3. Endocrinology 140, 2924-2927.
    • (1999) Endocrinology , vol.140 , pp. 2924-2927
    • Muff, R.1    Buhlmann, N.2    Fischer, J.A.3    Born, W.4
  • 3
  • 5
    • 27844496106 scopus 로고    scopus 로고
    • Receptor- activity-modifying proteins are required for forward trafficking of the calcium-sensing receptor to the plasma membrane
    • Bouschet, T., Martin, S., and Henley, J. M. (2005) Receptor- activity-modifying proteins are required for forward trafficking of the calcium-sensing receptor to the plasma membrane. J. Cell Sci. 118, 4709-4720.
    • (2005) J. Cell Sci , vol.118 , pp. 4709-4720
    • Bouschet, T.1    Martin, S.2    Henley, J.M.3
  • 7
    • 0034614398 scopus 로고    scopus 로고
    • Multiple ramp domains are required for generation of amylin receptor phenotype from the calcitonin receptor gene product
    • Zumpe, E. T., Tilakaratne, N., Fraser, N. J., Christopoulos, G., Foord, S. M., and Sexton, P. M. (2000) Multiple ramp domains are required for generation of amylin receptor phenotype from the calcitonin receptor gene product. Biochem. Biophys. Res. Commun. 267, 368-372.
    • (2000) Biochem. Biophys. Res. Commun , vol.267 , pp. 368-372
    • Zumpe, E.T.1    Tilakaratne, N.2    Fraser, N.J.3    Christopoulos, G.4    Foord, S.M.5    Sexton, P.M.6
  • 8
    • 0033013790 scopus 로고    scopus 로고
    • The amino terminus of receptor activity modifying proteins is a critical determinant of glycosylation state and ligand binding of calcitonin receptor-like receptor
    • Fraser, N. J., Wise, A., Brown, J., McLatchie, L. M., Main, M. J., and Foord, S. M. (1999) The amino terminus of receptor activity modifying proteins is a critical determinant of glycosylation state and ligand binding of calcitonin receptor-like receptor. Mol. Pharmacol. 55, 1054-1059.
    • (1999) Mol. Pharmacol , vol.55 , pp. 1054-1059
    • Fraser, N.J.1    Wise, A.2    Brown, J.3    McLatchie, L.M.4    Main, M.J.5    Foord, S.M.6
  • 9
    • 0038190946 scopus 로고    scopus 로고
    • The extracellular domain of receptor activity-modifying protein 1 is sufficient for calcitonin receptor-like receptor function
    • Fitzsimmons, T. J., Zhao, X., and Wank, S. A. (2003) The extracellular domain of receptor activity-modifying protein 1 is sufficient for calcitonin receptor-like receptor function. J. Biol. Chem. 278, 14313-14320.
    • (2003) J. Biol. Chem , vol.278 , pp. 14313-14320
    • Fitzsimmons, T.J.1    Zhao, X.2    Wank, S.A.3
  • 10
    • 16244383540 scopus 로고    scopus 로고
    • Mechanisms of peptide and nonpeptide ligand binding to class B G-protein-coupled receptors
    • Hoare, S. R. (2005) Mechanisms of peptide and nonpeptide ligand binding to class B G-protein-coupled receptors. Drug Discov. Today 10, 417-427.
    • (2005) Drug Discov. Today , vol.10 , pp. 417-427
    • Hoare, S.R.1
  • 11
    • 0345303705 scopus 로고    scopus 로고
    • The function of conserved cysteine residues in the extracellular domain of human receptor-activity-modifying protein
    • Steiner, S., Born, W., Fischer, J. A., and Muff, R. (2003) The function of conserved cysteine residues in the extracellular domain of human receptor-activity-modifying protein. FEBS Lett. 555, 285-290.
    • (2003) FEBS Lett , vol.555 , pp. 285-290
    • Steiner, S.1    Born, W.2    Fischer, J.A.3    Muff, R.4
  • 12
    • 0041823449 scopus 로고    scopus 로고
    • N-Glycosylation and conserved cysteine residues in RAMP3 play a critical role for the functional expression of CRLR/RAMP3 adrenomedullin receptor
    • Flahaut, M., Pfister, C., Rossier, B. C., and Firsov, D. (2003) N-Glycosylation and conserved cysteine residues in RAMP3 play a critical role for the functional expression of CRLR/RAMP3 adrenomedullin receptor. Biochemistry 42, 10333-10341.
    • (2003) Biochemistry , vol.42 , pp. 10333-10341
    • Flahaut, M.1    Pfister, C.2    Rossier, B.C.3    Firsov, D.4
  • 13
    • 0038265460 scopus 로고    scopus 로고
    • Identification of the human receptor activity-modifying protein 1 domains responsible for agonist binding specificity
    • Kuwasako, K., Kitamura, K., Nagoshi, Y., Cao, Y. N., and Eto, T. (2003) Identification of the human receptor activity-modifying protein 1 domains responsible for agonist binding specificity. J. Biol. Chem. 278, 22623-22630.
    • (2003) J. Biol. Chem , vol.278 , pp. 22623-22630
    • Kuwasako, K.1    Kitamura, K.2    Nagoshi, Y.3    Cao, Y.N.4    Eto, T.5
  • 14
    • 0037134498 scopus 로고    scopus 로고
    • Receptor activity-modifying protein 1 determines the species selectivity of non-peptide CGRP receptor antagonists
    • Mallee, J. J., Salvatore, C. A., LeBourdelles, B., Oliver, K. R., Longmore, J., Koblan, K. S., and Kane, S. A. (2002) Receptor activity-modifying protein 1 determines the species selectivity of non-peptide CGRP receptor antagonists. J. Biol. Chem. 277, 14294-14298.
    • (2002) J. Biol. Chem , vol.277 , pp. 14294-14298
    • Mallee, J.J.1    Salvatore, C.A.2    LeBourdelles, B.3    Oliver, K.R.4    Longmore, J.5    Koblan, K.S.6    Kane, S.A.7
  • 15
    • 33751073196 scopus 로고    scopus 로고
    • Determinants of 1-piperidinecarboxamide, N[2[[5amino-l-[[4(4-pyridinyl)l- piperazinyl]carbonyl]pentyl]amino]-1-[(3,5-dibromo-4-hydroxyphenyl)methyl] -2-oxoethyl]-4-(1,4-dihydro-2-oxo-3(2H)-quinazolinyl) (BIBN4096BS) affinity for calcitonin generelated peptide and amylin receptors the role of receptor activity modifying protein 1
    • Hay, D. L., Christopoulos, G., Christopoulos, A., and Sexton, P. M. (2006) Determinants of 1-piperidinecarboxamide, N[2[[5amino-l-[[4(4-pyridinyl)l- piperazinyl]carbonyl]pentyl]amino]-1-[(3,5-dibromo-4-hydroxyphenyl)methyl] -2-oxoethyl]-4-(1,4-dihydro-2-oxo-3(2H)-quinazolinyl) (BIBN4096BS) affinity for calcitonin generelated peptide and amylin receptors the role of receptor activity modifying protein 1. Mol. Pharmacol. 70, 1984-1991.
    • (2006) Mol. Pharmacol , vol.70 , pp. 1984-1991
    • Hay, D.L.1    Christopoulos, G.2    Christopoulos, A.3    Sexton, P.M.4
  • 16
    • 52949141814 scopus 로고    scopus 로고
    • Identification of N-terminal receptor activity-modifying protein residues important for calcitonin gene-related peptide, adrenomedullin, and amylin receptor function
    • Qi, T., Christopoulos, G., Bailey, R. J., Christopoulos, A., Sexton, P.M., and Hay, D. L. (2008) Identification of N-terminal receptor activity-modifying protein residues important for calcitonin gene-related peptide, adrenomedullin, and amylin receptor function. Mol. Pharmacol. 74, 1059-1071.
    • (2008) Mol. Pharmacol , vol.74 , pp. 1059-1071
    • Qi, T.1    Christopoulos, G.2    Bailey, R.J.3    Christopoulos, A.4    Sexton, P.M.5    Hay, D.L.6
  • 17
    • 33745700337 scopus 로고    scopus 로고
    • Characterization of the structure of RAMP1 by mutagenesis and molecular modelling
    • Simms, J., Hay, D. L., Wheatley, M., and Poyner, D. R. (2006) Characterization of the structure of RAMP1 by mutagenesis and molecular modelling. Biophys. J. 91, 662-669.
    • (2006) Biophys. J , vol.91 , pp. 662-669
    • Simms, J.1    Hay, D.L.2    Wheatley, M.3    Poyner, D.R.4
  • 19
    • 33747276441 scopus 로고    scopus 로고
    • Pharmacology of the human CGRP1 receptor in Cos 7 cells
    • Bailey, R. J., and Hay, D. L. (2006) Pharmacology of the human CGRP1 receptor in Cos 7 cells. Peptides 27, 1367-1375.
    • (2006) Peptides , vol.27 , pp. 1367-1375
    • Bailey, R.J.1    Hay, D.L.2
  • 20
    • 34347349008 scopus 로고    scopus 로고
    • Agonist-dependent consequences of proline to alanine substitution in the transmembrane helices of the calcitonin receptor
    • Bailey, R. J., and Hay, D. L. (2007) Agonist-dependent consequences of proline to alanine substitution in the transmembrane helices of the calcitonin receptor. Br. J. Pharmacol. 151, 678-687.
    • (2007) Br. J. Pharmacol , vol.151 , pp. 678-687
    • Bailey, R.J.1    Hay, D.L.2
  • 21
    • 2542445427 scopus 로고    scopus 로고
    • ConSurf: Identification of functional regions in proteins by surface-mapping of phylogenetic information
    • Glaser, F., Pupko, T., Paz, I., Bell, R. E., Bechor-Shental, D., Martz, E., and Ben-Tal, N. (2003) ConSurf: identification of functional regions in proteins by surface-mapping of phylogenetic information. Bioinformatics 19, 163-164.
    • (2003) Bioinformatics , vol.19 , pp. 163-164
    • Glaser, F.1    Pupko, T.2    Paz, I.3    Bell, R.E.4    Bechor-Shental, D.5    Martz, E.6    Ben-Tal, N.7
  • 22
    • 10844235653 scopus 로고    scopus 로고
    • Fernandez- Recio, J., Totrov, M., Skorodumov, C., and Abagyan, R. (2005) Optimal docking area: a new method for predicting protein-protein interaction sites. Proteins 58, 134-143. BI801869N
    • Fernandez- Recio, J., Totrov, M., Skorodumov, C., and Abagyan, R. (2005) Optimal docking area: a new method for predicting protein-protein interaction sites. Proteins 58, 134-143. BI801869N


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.