메뉴 건너뛰기




Volumn 27, Issue 2, 2003, Pages 103-114

Ab initio modelling of the N-terminal domain of the secretin receptors

Author keywords

Ab initio folding; Disulphide bridge; G protein coupled receptor; GLP1 receptor; Secretin family

Indexed keywords

HORMONES; MATHEMATICAL MODELS; MOLECULAR STRUCTURE; MUTAGENESIS;

EID: 0038348418     PISSN: 14769271     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1476-9271(03)00020-3     Document Type: Article
Times cited : (16)

References (48)
  • 2
    • 0028166611 scopus 로고
    • Folding polypeptide α-carbon backbones by distance geometry methods
    • Aszódi A., Taylor W.R. Folding polypeptide α-carbon backbones by distance geometry methods. Biopolymers. 34:1994;489-506.
    • (1994) Biopolymers , vol.34 , pp. 489-506
    • Aszódi, A.1    Taylor, W.R.2
  • 3
    • 0028221104 scopus 로고
    • Secondary structure formation in model polypeptide chains
    • Aszódi A., Taylor W.R. Secondary structure formation in model polypeptide chains. Protein Eng. 7:1994;633-644.
    • (1994) Protein Eng. , vol.7 , pp. 633-644
    • Aszódi, A.1    Taylor, W.R.2
  • 4
    • 0002066167 scopus 로고
    • Protein fold determination using a small number of distance restraints
    • H. Bohr, S. Brunak. Boca Raton, FL, USA: CRC Press
    • Aszódi A., Gradwell M.J., Taylor W.R. Protein fold determination using a small number of distance restraints. Bohr H., Brunak S. Protein Folds: A Distance Based Approach. 1995;85-97 CRC Press, Boca Raton, FL, USA.
    • (1995) Protein Folds: A Distance Based Approach , pp. 85-97
    • Aszódi, A.1    Gradwell, M.J.2    Taylor, W.R.3
  • 5
    • 0028987130 scopus 로고
    • Glucagon:glucagon-like peptide I receptor chimeras reveal domains that determine specificity of glucagon binding
    • Buggy J.J., Livingston J.N., Rabin D.U., Yoo-Warren H. Glucagon:glucagon-like peptide I receptor chimeras reveal domains that determine specificity of glucagon binding. J. Biol. Chem. 270:1995;7474-7478.
    • (1995) J. Biol. Chem. , vol.270 , pp. 7474-7478
    • Buggy, J.J.1    Livingston, J.N.2    Rabin, D.U.3    Yoo-Warren, H.4
  • 6
    • 0033105674 scopus 로고    scopus 로고
    • Molecular dynamics and accuracy of NMR structures: Effects of error bounds and data removal
    • Chalaoux F.R., O'Donoghue S.I., Nilges M. Molecular dynamics and accuracy of NMR structures: effects of error bounds and data removal. Proteins: Struct. Funct. Genet. 34:1999;453-463.
    • (1999) Proteins: Struct. Funct. Genet. , vol.34 , pp. 453-463
    • Chalaoux, F.R.1    O'Donoghue, S.I.2    Nilges, M.3
  • 8
    • 0032230249 scopus 로고    scopus 로고
    • Identification of binding domains of the growth hormone-releasing hormone receptor by analysis of mutant and chimeric receptor proteins
    • DeAlmeida V.I., Mayo K.E. Identification of binding domains of the growth hormone-releasing hormone receptor by analysis of mutant and chimeric receptor proteins. Mol. Endocrinol. 12:1998;750-765.
    • (1998) Mol. Endocrinol. , vol.12 , pp. 750-765
    • DeAlmeida, V.I.1    Mayo, K.E.2
  • 9
    • 0001691450 scopus 로고    scopus 로고
    • Protein fold determination from sparse distance constraints: The restrained generic protein direct Monte Carlo method
    • Debe D.A., Carlson M.J., Sadanobu J., Chan S.I., Goddard W.A. III. Protein fold determination from sparse distance constraints: the restrained generic protein direct Monte Carlo method. J. Phys. Chem. B103:1999;3001-3008.
    • (1999) J. Phys. Chem. , vol.B103 , pp. 3001-3008
    • Debe, D.A.1    Carlson, M.J.2    Sadanobu, J.3    Chan, S.I.4    Goddard W.A. III5
  • 11
    • 0033152909 scopus 로고    scopus 로고
    • Structure of the integral membrane domain of the GLP1 receptor
    • Frimurer T.M., Bywater R.P. Structure of the integral membrane domain of the GLP1 receptor. Proteins: Struct. Funct. Genet. 35:1999;375-386.
    • (1999) Proteins: Struct. Funct. Genet. , vol.35 , pp. 375-386
    • Frimurer, T.M.1    Bywater, R.P.2
  • 12
    • 0034254482 scopus 로고    scopus 로고
    • The N-terminal fragment of human parathyroid hormone receptor I constitutes a hormone binding domain and reveals a distinct disulfide pattern
    • Grauschopf U., Lilie H., Honold K., Wozny M., Reusch D., Esswein A., Schfer W., Rcknagel K.P., Rudolph R. The N-terminal fragment of human parathyroid hormone receptor I constitutes a hormone binding domain and reveals a distinct disulfide pattern. Biochemistry. 39:2000;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    Schfer, W.7    Rcknagel, K.P.8    Rudolph, R.9
  • 13
    • 0029961738 scopus 로고    scopus 로고
    • The amino terminal domain of the glucagon-like peptide-1 receptor is a critical determinant of subtype specificity
    • Graziano M.P., Hey P.J., Strader C.D. The amino terminal domain of the glucagon-like peptide-1 receptor is a critical determinant of subtype specificity. Recept. Channels. 4:1996;9-17.
    • (1996) Recept. Channels , vol.4 , pp. 9-17
    • Graziano, M.P.1    Hey, P.J.2    Strader, C.D.3
  • 16
    • 0033537993 scopus 로고    scopus 로고
    • GENTHREADER: An efficient and reliable protein fold recognition method for genomic sequences
    • Jones D.T. GENTHREADER: an efficient and reliable protein fold recognition method for genomic sequences. J. Mol. Biol. 287:1999;797-815.
    • (1999) J. Mol. Biol. , vol.287 , pp. 797-815
    • Jones, D.T.1
  • 17
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position-specific scoring matrices
    • Jones D.T. Protein secondary structure prediction based on position-specific scoring matrices. J. Mol. Biol. 292:1999;195-202.
    • (1999) J. Mol. Biol. , vol.292 , pp. 195-202
    • Jones, D.T.1
  • 18
    • 0034044314 scopus 로고    scopus 로고
    • The PSIPRED protein structure prediction server
    • Jones D.T. The PSIPRED protein structure prediction server. Bioinformatics. 16:2000;404-405.
    • (2000) Bioinformatics , vol.16 , pp. 404-405
    • Jones, D.T.1
  • 19
    • 0029804192 scopus 로고    scopus 로고
    • Identification and application of the concepts important for accurate and reliable protein secondary structure prediction
    • King R.D., Sternberg M.J.E. Identification and application of the concepts important for accurate and reliable protein secondary structure prediction. Protein Sci. 5:1996;2298-2310.
    • (1996) Protein Sci. , vol.5 , pp. 2298-2310
    • King, R.D.1    Sternberg, M.J.E.2
  • 20
    • 0025334980 scopus 로고
    • Improvements in protein secondary structure prediction by an enhanced neural network
    • Kneller D.G., Cohen F.E., Langridge R. Improvements in protein secondary structure prediction by an enhanced neural network. J. Mol. Biol. 214:1990;171-182.
    • (1990) J. Mol. Biol. , vol.214 , pp. 171-182
    • Kneller, D.G.1    Cohen, F.E.2    Langridge, R.3
  • 22
    • 0029846867 scopus 로고    scopus 로고
    • Relationship between protein structure and geometrical constraints
    • Lund O., Hansen J., Brunak S., Bohr J. Relationship between protein structure and geometrical constraints. Protein Sci. 5:1996;2217-2225.
    • (1996) Protein Sci. , vol.5 , pp. 2217-2225
    • Lund, O.1    Hansen, J.2    Brunak, S.3    Bohr, J.4
  • 23
    • 0038256152 scopus 로고    scopus 로고
    • Ph.D. thesis, Laboratory of Mathematical Biology, National Institute for Medical Research (MRC), London, affiliated to University College, University of London
    • Munro, R.E.J., 1999. Protein Structure Prediction and Modelling. Ph.D. thesis, Laboratory of Mathematical Biology, National Institute for Medical Research (MRC), London, affiliated to University College, University of London.
    • (1999) Protein Structure Prediction and Modelling
    • Munro, R.E.J.1
  • 24
    • 0028276459 scopus 로고
    • A common step for signal transduction in G protein-coupled receptors
    • Oliveira L., Paiva A.C.M., Sander C., Vriend G. A common step for signal transduction in G protein-coupled receptors. Trends Pharmacol. Sci. 15:1994;170-172.
    • (1994) Trends Pharmacol. Sci. , vol.15 , pp. 170-172
    • Oliveira, L.1    Paiva, A.C.M.2    Sander, C.3    Vriend, G.4
  • 25
    • 0030821675 scopus 로고    scopus 로고
    • Correlated mutations contain information about protein-protein interaction
    • Pazos F., Helmer-Citterich M., Ausiello G., Valencia A. Correlated mutations contain information about protein-protein interaction. J. Mol. Biol. 271:1997;511-523.
    • (1997) J. Mol. Biol. , vol.271 , pp. 511-523
    • Pazos, F.1    Helmer-Citterich, M.2    Ausiello, G.3    Valencia, A.4
  • 26
    • 0037474530 scopus 로고    scopus 로고
    • Modelling zinc-binding proteins with GADGET: Genetic algorithm and distance geometry for exploring topology
    • Petersen K., Taylor W.R. Modelling zinc-binding proteins with GADGET: genetic algorithm and distance geometry for exploring topology. J. Mol. Biol. 325:2003;1039-1059.
    • (2003) J. Mol. Biol. , vol.325 , pp. 1039-1059
    • Petersen, K.1    Taylor, W.R.2
  • 27
    • 0030743758 scopus 로고    scopus 로고
    • Effectiveness of correlation analysis in identifying protein residues undergoing correlated evolution
    • Pollock D.D., Taylor W.R. Effectiveness of correlation analysis in identifying protein residues undergoing correlated evolution. Protein Eng. 10:1997;647-657.
    • (1997) Protein Eng. , vol.10 , pp. 647-657
    • Pollock, D.D.1    Taylor, W.R.2
  • 28
    • 0033582946 scopus 로고    scopus 로고
    • Coevolving protein residues: Maximum likelihood identification and relationship to structure
    • Pollock D.D., Taylor W.R., Goldman N. Coevolving protein residues: maximum likelihood identification and relationship to structure. J. Mol. Biol. 287:1999;187-198.
    • (1999) J. Mol. Biol. , vol.287 , pp. 187-198
    • Pollock, D.D.1    Taylor, W.R.2    Goldman, N.3
  • 29
    • 0030820210 scopus 로고    scopus 로고
    • Extracellular cysteines of the corticotropin-releasing factor (CRF) receptor are critical for ligand binding
    • Qi L.J., Leung A.T., Xiong Y.T., Marx K.A., Abou-Samra A.B. Extracellular cysteines of the corticotropin-releasing factor (CRF) receptor are critical for ligand binding. Biochemistry. 36:1997;12442-12448.
    • (1997) Biochemistry , vol.36 , pp. 12442-12448
    • Qi, L.J.1    Leung, A.T.2    Xiong, Y.T.3    Marx, K.A.4    Abou-Samra, A.B.5
  • 30
    • 0017387723 scopus 로고
    • β-Sheet topology and the relatedness of proteins
    • Richardson J.S. β-Sheet topology and the relatedness of proteins. Nature. 268:1977;495-500.
    • (1977) Nature , vol.268 , pp. 495-500
    • Richardson, J.S.1
  • 31
    • 0027291015 scopus 로고
    • Prediction of protein secondary structure at better than 70-percent accuracy
    • Rost B., Sander C. Prediction of protein secondary structure at better than 70-percent accuracy. J. Mol. Biol. 232:1993;584-599.
    • (1993) J. Mol. Biol. , vol.232 , pp. 584-599
    • Rost, B.1    Sander, C.2
  • 32
    • 0028965118 scopus 로고
    • Prediction of protein secondary structure by combining nearest-neighbor algorithms and multiple sequence alignments
    • Salamov A.A., Solovyev V.V. Prediction of protein secondary structure by combining nearest-neighbor algorithms and multiple sequence alignments. J. Mol. Biol. 247:1995;11-15.
    • (1995) J. Mol. Biol. , vol.247 , pp. 11-15
    • Salamov, A.A.1    Solovyev, V.V.2
  • 33
    • 0028084754 scopus 로고
    • Can three-dimensional contacts in protein structures be predicted by analysis of correlated mutations
    • Shindyalov I.N., Kolchanov N.A., Sander C. Can three-dimensional contacts in protein structures be predicted by analysis of correlated mutations. Protein Eng. 7:1994;349-358.
    • (1994) Protein Eng. , vol.7 , pp. 349-358
    • Shindyalov, I.N.1    Kolchanov, N.A.2    Sander, C.3
  • 34
    • 0024245156 scopus 로고
    • A flexible method to align large numbers of biological sequences
    • Taylor W.R. A flexible method to align large numbers of biological sequences. J. Mol. Evol. 28:1988;161-169.
    • (1988) J. Mol. Evol. , vol.28 , pp. 161-169
    • Taylor, W.R.1
  • 35
    • 0030825816 scopus 로고    scopus 로고
    • Residual colours: A proposal for aminochromography
    • Taylor W.R. Residual colours: a proposal for aminochromography. Protein Eng. 10:1997;743-746.
    • (1997) Protein Eng. , vol.10 , pp. 743-746
    • Taylor, W.R.1
  • 36
    • 0032540981 scopus 로고    scopus 로고
    • Dynamic databank searching with templates and multiple alignment
    • Taylor W.R. Dynamic databank searching with templates and multiple alignment. J. Mol. Biol. 280:1998;375-406.
    • (1998) J. Mol. Biol. , vol.280 , pp. 375-406
    • Taylor, W.R.1
  • 37
    • 0034710671 scopus 로고    scopus 로고
    • A deeply knotted protein and how it might fold
    • Taylor W.R. A deeply knotted protein and how it might fold. Nature. 406:2000;916-919.
    • (2000) Nature , vol.406 , pp. 916-919
    • Taylor, W.R.1
  • 38
    • 0037061460 scopus 로고    scopus 로고
    • A periodic table for protein structure
    • Taylor W.R. A periodic table for protein structure. Nature. 416:2002;657-660.
    • (2002) Nature , vol.416 , pp. 657-660
    • Taylor, W.R.1
  • 40
    • 0027952860 scopus 로고
    • Compensating changes in protein multiple sequence alignments
    • Taylor W.R., Hatrick K. Compensating changes in protein multiple sequence alignments. Protein Eng. 7:1994;341-348.
    • (1994) Protein Eng. , vol.7 , pp. 341-348
    • Taylor, W.R.1    Hatrick, K.2
  • 41
    • 0006513703 scopus 로고
    • Modelling and predicting α-helical trans-membrane structures
    • H. Bohr, & S. Brunak. Boca Raton, FL, USA: CRC Press
    • Taylor W.R., Jones D.T. Modelling and predicting α-helical trans-membrane structures. Bohr H., Brunak S. Protein Folds: a Distance Based Approach. 1995;283-293 CRC Press, Boca Raton, FL, USA.
    • (1995) Protein Folds: A Distance Based Approach , pp. 283-293
    • Taylor, W.R.1    Jones, D.T.2
  • 42
  • 43
    • 0029659025 scopus 로고    scopus 로고
    • Exchange of W39 by a within the N-terminal extracellular domain of the GLP-1 receptor results in a loss of receptor function
    • Van Eyll B., Göke B., Wilmen A., Göke R. Exchange of W39 by a within the N-terminal extracellular domain of the GLP-1 receptor results in a loss of receptor function. Peptides. 17:1996;565-570.
    • (1996) Peptides , vol.17 , pp. 565-570
    • Van Eyll, B.1    Göke, B.2    Wilmen, A.3    Göke, R.4
  • 44
    • 0029016549 scopus 로고
    • Properties of chimeric secretin and vip receptor proteins indicate the importance of the N-terminal domain for ligand discrimination
    • Vilardaga J.P., De Neef R., Di Paolo E., Bollen A., Waelbroeck M., Robberecht P. Properties of chimeric secretin and vip receptor proteins indicate the importance of the N-terminal domain for ligand discrimination. Biochem. Biophys. Res. Commun. 211:1995;885-891.
    • (1995) Biochem. Biophys. Res. Commun. , vol.211 , pp. 885-891
    • Vilardaga, J.P.1    De Neef, R.2    Di Paolo, E.3    Bollen, A.4    Waelbroeck, M.5    Robberecht, P.6
  • 45
    • 0030941907 scopus 로고    scopus 로고
    • Mutational analysis of extracellular cysteine residues of rat secretin receptor shows that disulfide bridges are essential for receptor function
    • Vilardaga J.P., Di Paolo E., Bialek C., De Neef P., Waelbroeck M., Bollen A., Robberecht P. Mutational analysis of extracellular cysteine residues of rat secretin receptor shows that disulfide bridges are essential for receptor function. Eur. J. Biochem. 246:1997;173-180.
    • (1997) Eur. J. Biochem. , vol.246 , pp. 173-180
    • Vilardaga, J.P.1    Di Paolo, E.2    Bialek, C.3    De Neef, P.4    Waelbroeck, M.5    Bollen, A.6    Robberecht, P.7
  • 46
    • 0025398721 scopus 로고
    • WHAT IF: A molecular modeling and drug design program
    • Vriend G. WHAT IF: a molecular modeling and drug design program. J. Mol. Graph. 8:1990;52-56.
    • (1990) J. Mol. Graph. , vol.8 , pp. 52-56
    • Vriend, G.1
  • 47
    • 0030602177 scopus 로고    scopus 로고
    • The isolated N-terminal extracellular domain of the glucagon-like peptide-1
    • Wilmen A., Göke B., Göke R. The isolated N-terminal extracellular domain of the glucagon-like peptide-1. FEBS Lett. 398:1996;43-47.
    • (1996) FEBS Lett. , vol.398 , pp. 43-47
    • Wilmen, A.1    Göke, B.2    Göke, R.3
  • 48
    • 0030921314 scopus 로고    scopus 로고
    • Five out of six tryptophan residues in the N-terminal extracellular domain of the rat GLP-1 receptor are essential for its ability to bind GLP-1
    • Wilmen A., Van Eyll B., Göke B., Göke R. Five out of six tryptophan residues in the N-terminal extracellular domain of the rat GLP-1 receptor are essential for its ability to bind GLP-1. Peptides. 18:1997;301-305.
    • (1997) Peptides , vol.18 , pp. 301-305
    • Wilmen, A.1    Van Eyll, B.2    Göke, B.3    Göke, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.