메뉴 건너뛰기




Volumn 288, Issue 39, 2013, Pages 28138-28151

The relaxin receptor (RXFP1) utilizes hydrophobic moieties on a signaling surface of its N-terminal low density lipoprotein class a module to mediate receptor activation

Author keywords

[No Author keywords available]

Indexed keywords

CLASS A; DRUG DEVELOPMENT; HYDROPHOBIC MOIETIES; LOW DENSITY LIPOPROTEINS; N TERMINUS; N-TERMINALS; RECEPTOR ACTIVATION; SIDE-CHAINS;

EID: 84884756868     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.499640     Document Type: Article
Times cited : (23)

References (43)
  • 3
    • 0042836864 scopus 로고    scopus 로고
    • New insights into the evolution of the relaxin-LGR signaling system
    • Hsu, S. Y. (2003) New insights into the evolution of the relaxin-LGR signaling system. Trends Endocrinol. Metab. 14, 303-309
    • (2003) Trends Endocrinol. Metab. , vol.14 , pp. 303-309
    • Hsu, S.Y.1
  • 4
    • 0028354924 scopus 로고
    • Characterization of two relaxin genes in the chimpanzee
    • Evans, B. A., Fu, P., and Tregear, G. W. (1994) Characterization of two relaxin genes in the chimpanzee. J. Endocrinol. 140, 385-392
    • (1994) J. Endocrinol. , vol.140 , pp. 385-392
    • Evans, B.A.1    Fu, P.2    Tregear, G.W.3
  • 7
    • 0029126464 scopus 로고
    • Relaxin-induced increased coronary flow through stimulation of nitric oxide production
    • Bani-Sacchi, T., Bigazzi, M., Bani, D., Mannaioni, P. F., and Masini, E. (1995) Relaxin-induced increased coronary flow through stimulation of nitric oxide production. Br. J. Pharmacol. 116, 1589-1594
    • (1995) Br. J. Pharmacol. , vol.116 , pp. 1589-1594
    • Bani-Sacchi, T.1    Bigazzi, M.2    Bani, D.3    Mannaioni, P.F.4    Masini, E.5
  • 8
    • 0031810556 scopus 로고    scopus 로고
    • Relaxin activates the L-arginine-nitric oxide pathway in vascular smooth muscle cells in culture
    • Bani, D., Failli, P., Bello, M. G., Thiemermann, C., Bani Sacchi, T., Bigazzi, M., and Masini, E. (1998) Relaxin activates the L-arginine-nitric oxide pathway in vascular smooth muscle cells in culture. Hypertension 31, 1240-1247
    • (1998) Hypertension , vol.31 , pp. 1240-1247
    • Bani, D.1    Failli, P.2    Bello, M.G.3    Thiemermann, C.4    Bani Sacchi, T.5    Bigazzi, M.6    Masini, E.7
  • 9
    • 0037428061 scopus 로고    scopus 로고
    • Relaxin, a pregnancy hormone, is a functional endothelin-1 antagonist: Attenuation of endothelin-1-mediated vasoconstriction by stimulation of endothelin type-B receptor expression via ERK-1/2 and nuclear factor-B
    • Dschietzig, T., Bartsch, C., Richter, C., Laule, M., Baumann, G., and Stangl, K. (2003) Relaxin, a pregnancy hormone, is a functional endothelin-1 antagonist: attenuation of endothelin-1-mediated vasoconstriction by stimulation of endothelin type-B receptor expression via ERK-1/2 and nuclear factor-B. Circ. Res. 92, 32-40
    • (2003) Circ. Res. , vol.92 , pp. 32-40
    • Dschietzig, T.1    Bartsch, C.2    Richter, C.3    Laule, M.4    Baumann, G.5    Stangl, K.6
  • 14
    • 33644589069 scopus 로고    scopus 로고
    • International Union of Pharmacology LVII: Recommendations for the nomenclature of receptors for relaxin family peptides
    • Bathgate, R. A., Ivell, R., Sanborn, B. M., Sherwood, O. D., and Summers, R. J. (2006) International Union of Pharmacology LVII: recommendations for the nomenclature of receptors for relaxin family peptides. Pharmacol. Rev. 58, 7-31
    • (2006) Pharmacol. Rev. , vol.58 , pp. 7-31
    • Bathgate, R.A.1    Ivell, R.2    Sanborn, B.M.3    Sherwood, O.D.4    Summers, R.J.5
  • 15
    • 17144426920 scopus 로고    scopus 로고
    • The trap-like relaxin-binding site of the leucine-rich G-protein-coupled receptor 7
    • Büllesbach, E. E., and Schwabe, C. (2005) The trap-like relaxin-binding site of the leucine-rich G-protein-coupled receptor 7. J. Biol. Chem. 280, 14051-14056
    • (2005) J. Biol. Chem. , vol.280 , pp. 14051-14056
    • Büllesbach, E.E.1    Schwabe, C.2
  • 17
    • 84868087243 scopus 로고    scopus 로고
    • The different ligand-binding modes of relaxin family peptide receptors RXFP1 and RXFP2
    • Scott, D. J., Rosengren, K. J., and Bathgate, R. A. (2012) The different ligand-binding modes of relaxin family peptide receptors RXFP1 and RXFP2. Mol. Endocrinol. 26, 1896-1906
    • (2012) Mol. Endocrinol. , vol.26 , pp. 1896-1906
    • Scott, D.J.1    Rosengren, K.J.2    Bathgate, R.A.3
  • 18
    • 33845933437 scopus 로고    scopus 로고
    • Characterization of novel splice variants of LGR7 and LGR8 reveals that receptor signaling is mediated by their unique low density lipoprotein class A modules
    • Scott, D. J., Layfield, S., Yan, Y., Sudo, S., Hsueh, A. J., Tregear, G. W., and Bathgate, R. A. (2006) Characterization of novel splice variants of LGR7 and LGR8 reveals that receptor signaling is mediated by their unique low density lipoprotein class A modules. J. Biol. Chem. 281, 34942-34954
    • (2006) J. Biol. Chem. , vol.281 , pp. 34942-34954
    • Scott, D.J.1    Layfield, S.2    Yan, Y.3    Sudo, S.4    Hsueh, A.J.5    Tregear, G.W.6    Bathgate, R.A.7
  • 19
    • 33947501041 scopus 로고    scopus 로고
    • The NMR solution structure of the relaxin (RXFP1) receptor lipoprotein receptor class A module and identification of key residues in the N-terminal region of the module that mediate receptor activation
    • Hopkins, E. J., Layfield, S., Ferraro, T., Bathgate, R. A., and Gooley, P. R. (2007) The NMR solution structure of the relaxin (RXFP1) receptor lipoprotein receptor class A module and identification of key residues in the N-terminal region of the module that mediate receptor activation. J. Biol. Chem. 282, 4172-4184
    • (2007) J. Biol. Chem. , vol.282 , pp. 4172-4184
    • Hopkins, E.J.1    Layfield, S.2    Ferraro, T.3    Bathgate, R.A.4    Gooley, P.R.5
  • 20
    • 33847071711 scopus 로고    scopus 로고
    • The lowdensity lipoprotein class A module of the relaxin receptor (leucine-rich repeat containing G-protein coupled receptor 7): Its role in signaling and trafficking to the cell membrane
    • Kern, A., Agoulnik, A. I., and Bryant-Greenwood, G. D. (2007) The lowdensity lipoprotein class A module of the relaxin receptor (leucine-rich repeat containing G-protein coupled receptor 7): its role in signaling and trafficking to the cell membrane. Endocrinology 148, 1181-1194
    • (2007) Endocrinology , vol.148 , pp. 1181-1194
    • Kern, A.1    Agoulnik, A.I.2    Bryant-Greenwood, G.D.3
  • 21
    • 41149137180 scopus 로고    scopus 로고
    • Overview of the retrovirus transduction system
    • Chapter 9, Unit 9.9
    • Cepko, C., and Pear, W. (2001) Overview of the retrovirus transduction system. Curr. Protoc. Mol. Biol. Chapter 9, Unit 9.9
    • (2001) Curr. Protoc. Mol. Biol.
    • Cepko, C.1    Pear, W.2
  • 22
    • 33845939640 scopus 로고    scopus 로고
    • Comparison of signaling pathways activated by the relaxin family peptide receptors, RXFP1 and RXFP2, using reporter genes
    • Halls, M. L., Bathgate, R. A., and Summers, R. J. (2007) Comparison of signaling pathways activated by the relaxin family peptide receptors, RXFP1 and RXFP2, using reporter genes. J. Pharmacol. Exp. Ther. 320, 281-290
    • (2007) J. Pharmacol. Exp. Ther. , vol.320 , pp. 281-290
    • Halls, M.L.1    Bathgate, R.A.2    Summers, R.J.3
  • 23
    • 46049108362 scopus 로고    scopus 로고
    • Identification of the N-linked glycosylation sites of the human relaxin receptor and effect of glycosylation on receptor function
    • Yan, Y., Scott, D. J., Wilkinson, T. N., Ji, J., Tregear, G. W., and Bathgate, R. A. (2008) Identification of the N-linked glycosylation sites of the human relaxin receptor and effect of glycosylation on receptor function. Biochemistry 47, 6953-6968
    • (2008) Biochemistry , vol.47 , pp. 6953-6968
    • Yan, Y.1    Scott, D.J.2    Wilkinson, T.N.3    Ji, J.4    Tregear, G.W.5    Bathgate, R.A.6
  • 24
    • 3843146246 scopus 로고    scopus 로고
    • An efficient one-step site-directed and site-saturation mutagenesis protocol
    • Zheng, L., Baumann, U., and Reymond, J.-L. (2004) An efficient one-step site-directed and site-saturation mutagenesis protocol. Nucleic Acids Res. 32, e115
    • (2004) Nucleic Acids Res. , vol.32
    • Zheng, L.1    Baumann, U.2    Reymond, J.-L.3
  • 25
    • 0031627465 scopus 로고    scopus 로고
    • An efficient and cost-effective isotope labeling protocol for proteins expressed in Escherichia coli
    • Cai, M., Huang, Y., Sakaguchi, K., Clore, G. M., Gronenborn, A. M., and Craigie, R. (1998) An efficient and cost-effective isotope labeling protocol for proteins expressed in Escherichia coli. J. Biomol. NMR 11, 97-102
    • (1998) J. Biomol. NMR , vol.11 , pp. 97-102
    • Cai, M.1    Huang, Y.2    Sakaguchi, K.3    Clore, G.M.4    Gronenborn, A.M.5    Craigie, R.6
  • 27
    • 46949106433 scopus 로고    scopus 로고
    • Automated sequence-specific protein NMR assignment using the memetic algorithm MATCH
    • Volk, J., Herrmann, T., and Wüthrich, K. (2008) Automated sequence-specific protein NMR assignment using the memetic algorithm MATCH. J. Biomol. NMR 41, 127-138
    • (2008) J. Biomol. NMR , vol.41 , pp. 127-138
    • Volk, J.1    Herrmann, T.2    Wüthrich, K.3
  • 28
    • 51749107733 scopus 로고    scopus 로고
    • Automated amino acid side-chain NMR assignment of proteins using 13Cand 15N-resolved 3D [1H, 1H]-NOESY
    • Fiorito, F., Herrmann, T., Damberger, F. F., and Wüthrich, K. (2008) Automated amino acid side-chain NMR assignment of proteins using 13Cand 15N-resolved 3D [1H, 1H]-NOESY. J. Biomol. NMR 42, 23-33
    • (2008) J. Biomol. NMR , vol.42 , pp. 23-33
    • Fiorito, F.1    Herrmann, T.2    Damberger, F.F.3    Wüthrich, K.4
  • 29
    • 0036308102 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA
    • Herrmann, T., Güntert, P., and Wüthrich, K. (2002) Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA. J. Mol. Biol. 319, 209-227
    • (2002) J. Mol. Biol. , vol.319 , pp. 209-227
    • Herrmann, T.1    Güntert, P.2    Wüthrich, K.3
  • 30
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structure calculation with the new program DYANA
    • Güntert, P., Mumenthaler, C., and Wüthrich, K. (1997) Torsion angle dynamics for NMR structure calculation with the new program DYANA. J. Mol. Biol. 273, 283-298
    • (1997) J. Mol. Biol. , vol.273 , pp. 283-298
    • Güntert, P.1    Mumenthaler, C.2    Wüthrich, K.3
  • 31
    • 0030759357 scopus 로고    scopus 로고
    • Molecular basis of familial hypercholesterolaemia from structure of LDL receptor module
    • Fass, D., Blacklow, S., Kim, P. S., and Berger, J. M. (1997) Molecular basis of familial hypercholesterolaemia from structure of LDL receptor module. Nature 388, 691-693
    • (1997) Nature , vol.388 , pp. 691-693
    • Fass, D.1    Blacklow, S.2    Kim, P.S.3    Berger, J.M.4
  • 32
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi, R., Billeter, M., and Wüthrich, K. (1996) MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14, 51-55
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 34
    • 23644432627 scopus 로고    scopus 로고
    • The human LGR7 low-density lipoprotein class A module requires calcium for structure
    • Hopkins, E. J., Bathgate, R. A., and Gooley, P. R. (2005) The human LGR7 low-density lipoprotein class A module requires calcium for structure. Ann. N.Y. Acad. Sci. 1041, 27-34
    • (2005) Ann. N.Y. Acad. Sci. , vol.1041 , pp. 27-34
    • Hopkins, E.J.1    Bathgate, R.A.2    Gooley, P.R.3
  • 35
    • 0032483116 scopus 로고    scopus 로고
    • Folding, calcium binding, and structural characterization of a concatemer of the first and second ligand-binding modules of the low-density lipoprotein receptor
    • Bieri, S., Atkins, A. R., Lee, H. T., Winzor, D. J., Smith, R., and Kroon, P. A. (1998) Folding, calcium binding, and structural characterization of a concatemer of the first and second ligand-binding modules of the low-density lipoprotein receptor. Biochemistry 37, 10994-11002
    • (1998) Biochemistry , vol.37 , pp. 10994-11002
    • Bieri, S.1    Atkins, A.R.2    Lee, H.T.3    Winzor, D.J.4    Smith, R.5    Kroon, P.A.6
  • 36
    • 0028866813 scopus 로고
    • Threedimensional structure of the second cysteine-rich repeat from the human low-density lipoprotein receptor
    • Daly, N. L., Djordjevic, J. T., Kroon, P. A., and Smith, R. (1995) Threedimensional structure of the second cysteine-rich repeat from the human low-density lipoprotein receptor. Biochemistry 34, 14474-14481
    • (1995) Biochemistry , vol.34 , pp. 14474-14481
    • Daly, N.L.1    Djordjevic, J.T.2    Kroon, P.A.3    Smith, R.4
  • 37
    • 33846018526 scopus 로고    scopus 로고
    • T222P mutation of the insulin-like 3 hormone receptor LGR8 is associated with testicular maldescent and hinders receptor expression on the cell surface membrane
    • Bogatcheva, N. V., Ferlin, A., Feng, S., Truong, A., Gianesello, L., Foresta, C., and Agoulnik, A. I. (2007) T222P mutation of the insulin-like 3 hormone receptor LGR8 is associated with testicular maldescent and hinders receptor expression on the cell surface membrane. Am. J. Physiol. Endocrinol. Metab. 292, E138-E144
    • (2007) Am. J. Physiol. Endocrinol. Metab. , vol.292
    • Bogatcheva, N.V.1    Ferlin, A.2    Feng, S.3    Truong, A.4    Gianesello, L.5    Foresta, C.6    Agoulnik, A.I.7
  • 39
    • 77649144078 scopus 로고    scopus 로고
    • Structural basis for specific recognition of reelin by its receptors
    • Yasui, N., Nogi, T., and Takagi, J. (2010) Structural basis for specific recognition of reelin by its receptors. Structure 18, 320-331
    • (2010) Structure , vol.18 , pp. 320-331
    • Yasui, N.1    Nogi, T.2    Takagi, J.3
  • 40
    • 33646046808 scopus 로고    scopus 로고
    • Structure of an LDLRRAP complex reveals a general mode for ligand recognition by lipoprotein receptors
    • Fisher, C., Beglova, N., and Blacklow, S. C. (2006) Structure of an LDLRRAP complex reveals a general mode for ligand recognition by lipoprotein receptors. Mol. Cell 22, 277-283
    • (2006) Mol. Cell , vol.22 , pp. 277-283
    • Fisher, C.1    Beglova, N.2    Blacklow, S.C.3
  • 41
    • 84873671045 scopus 로고    scopus 로고
    • Gentamicin binds to the megalin receptor as a competitive inhibitor using the common ligand binding motif of complement type repeats: Insight from the NMR structure of the 10th complement type repeat domain alone and in complex with gentamicin
    • Dagil, R., O'Shea, C., Nykjær, A., Bonvin, A. M., and Kragelund, B. B. (2013) Gentamicin binds to the megalin receptor as a competitive inhibitor using the common ligand binding motif of complement type repeats: insight from the NMR structure of the 10th complement type repeat domain alone and in complex with gentamicin. J. Biol. Chem. 288, 4424-4435
    • (2013) J. Biol. Chem. , vol.288 , pp. 4424-4435
    • Dagil, R.1    O'shea, C.2    Nykjær, A.3    Bonvin, A.M.4    Kragelund, B.B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.