메뉴 건너뛰기




Volumn 47, Issue 48, 2008, Pages 12900-12909

High-affinity insulin binding: Insulin interacts with two receptor ligand binding sites

Author keywords

[No Author keywords available]

Indexed keywords

AMINES; BINDING ENERGY; BIOCHEMISTRY; FLOW INTERACTIONS; HORMONES; INSULIN; LIGANDS; SCANNING;

EID: 57049086436     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi801693h     Document Type: Article
Times cited : (75)

References (49)
  • 2
    • 0036782071 scopus 로고    scopus 로고
    • Structural biology of insulin and IGF1 receptors: Implications for drug design
    • De Meyts, P., and Whittaker, J. (2002) Structural biology of insulin and IGF1 receptors: implications for drug design. Nat. Rev. Drug Discovery 1, 769-783.
    • (2002) Nat. Rev. Drug Discovery , vol.1 , pp. 769-783
    • De Meyts, P.1    Whittaker, J.2
  • 3
    • 29244462334 scopus 로고    scopus 로고
    • Insulin signaling and the regulation of glucose transport
    • Chang, L., Chiang, S. H., and Saltiel, A. R. (2004) Insulin signaling and the regulation of glucose transport. Mol. Med. 10, 65-71.
    • (2004) Mol. Med , vol.10 , pp. 65-71
    • Chang, L.1    Chiang, S.H.2    Saltiel, A.R.3
  • 4
    • 33244464562 scopus 로고    scopus 로고
    • Critical nodes in signalling pathways: Insights into insulin action
    • Taniguchi, C. M., Emanuelli, B., and Kahn, C. R. (2006) Critical nodes in signalling pathways: Insights into insulin action. Nat. Rev. Mol. Cell Biol. 7, 85-96.
    • (2006) Nat. Rev. Mol. Cell Biol , vol.7 , pp. 85-96
    • Taniguchi, C.M.1    Emanuelli, B.2    Kahn, C.R.3
  • 5
    • 0032932822 scopus 로고    scopus 로고
    • Insulin receptor isoform A, a newly recognized, high-affinity insulin-like growth factor II receptor in fetal and cancer cells
    • Frasca, F., Pandini, G., Scalia, P., Sciacca, L., Mineo, R., Costantino, A., Goldfine, I. D., Belfiore, A., and Vigneri, R. (1999) Insulin receptor isoform A, a newly recognized, high-affinity insulin-like growth factor II receptor in fetal and cancer cells. Mol. Cell. Biol. 19, 3278-3288.
    • (1999) Mol. Cell. Biol , vol.19 , pp. 3278-3288
    • Frasca, F.1    Pandini, G.2    Scalia, P.3    Sciacca, L.4    Mineo, R.5    Costantino, A.6    Goldfine, I.D.7    Belfiore, A.8    Vigneri, R.9
  • 6
    • 14944377711 scopus 로고    scopus 로고
    • IGF-II binding to insulin receptor isoform A induces a partially different gene expression profile from insulin binding
    • Pandini, G., Conte, E., Medico, E., Sciacca, L., Vigneri, R., and Belfiore, A. (2004) IGF-II binding to insulin receptor isoform A induces a partially different gene expression profile from insulin binding. Ann. N.Y. Acad. Sci. 1028, 450-456.
    • (2004) Ann. N.Y. Acad. Sci , vol.1028 , pp. 450-456
    • Pandini, G.1    Conte, E.2    Medico, E.3    Sciacca, L.4    Vigneri, R.5    Belfiore, A.6
  • 7
    • 34248180625 scopus 로고    scopus 로고
    • Differential activation of insulin receptor substrates 1 and 2 by insulin-like growth factor-activated insulin receptors
    • Denley, A., Carroll, J. M., Brierley, G. V., Cosgrove, L., Wallace, J., Forbes, B., and Roberts, C. T., Jr. (2007) Differential activation of insulin receptor substrates 1 and 2 by insulin-like growth factor-activated insulin receptors. Mol. Cell. Biol. 27, 3569-3577.
    • (2007) Mol. Cell. Biol , vol.27 , pp. 3569-3577
    • Denley, A.1    Carroll, J.M.2    Brierley, G.V.3    Cosgrove, L.4    Wallace, J.5    Forbes, B.6    Roberts Jr., C.T.7
  • 8
    • 36849015259 scopus 로고    scopus 로고
    • Activation of the insulin receptor by insulin and a synthetic peptide leads to divergent metabolic and mitogenic signaling and responses
    • Jensen, M., Hansen, B., De Meyts, P., Schaffer, L., and Urso, B. (2007) Activation of the insulin receptor by insulin and a synthetic peptide leads to divergent metabolic and mitogenic signaling and responses. J. Biol. Chem. 282, 35179-35186.
    • (2007) J. Biol. Chem , vol.282 , pp. 35179-35186
    • Jensen, M.1    Hansen, B.2    De Meyts, P.3    Schaffer, L.4    Urso, B.5
  • 9
    • 0023262816 scopus 로고
    • The insulin receptor. Structural basis for high affinity ligand binding
    • Boni-Schnetzler, M., Scott, W., Waugh, S. M., DiBella, E., and Pilch, P. F. (1987) The insulin receptor. Structural basis for high affinity ligand binding. J. Biol. Chem. 262, 8395-8401.
    • (1987) J. Biol. Chem , vol.262 , pp. 8395-8401
    • Boni-Schnetzler, M.1    Scott, W.2    Waugh, S.M.3    DiBella, E.4    Pilch, P.F.5
  • 10
    • 0022441892 scopus 로고
    • The nonclassical insulin binding of insulin receptors from rat liver is due to the presence of two interacting alpha-subunits in the receptor complex
    • Deger, A., Kramer, H., Rapp, R., Koch, R., and Weber, U. (1986) The nonclassical insulin binding of insulin receptors from rat liver is due to the presence of two interacting alpha-subunits in the receptor complex. Biochem. Biophys. Res. Commun. 135, 458-464.
    • (1986) Biochem. Biophys. Res. Commun , vol.135 , pp. 458-464
    • Deger, A.1    Kramer, H.2    Rapp, R.3    Koch, R.4    Weber, U.5
  • 11
    • 0023267760 scopus 로고
    • Isolation of functional alpha beta heterodimers from the purified human placental alpha 2 beta 2 heterotetrameric insulin receptor complex. A structural basis for insulin binding heterogeneity
    • Sweet, L. J., Morrison, B. D., and Pessin, J. E. (1987) Isolation of functional alpha beta heterodimers from the purified human placental alpha 2 beta 2 heterotetrameric insulin receptor complex. A structural basis for insulin binding heterogeneity. J. Biol. Chem. 262, 6939-6942.
    • (1987) J. Biol. Chem , vol.262 , pp. 6939-6942
    • Sweet, L.J.1    Morrison, B.D.2    Pessin, J.E.3
  • 13
    • 0033597852 scopus 로고    scopus 로고
    • Proteolytic processing in the secretory pathway
    • Zhou, A., Webb, G., Zhu, X., and Steiner, D. F. (1999) Proteolytic processing in the secretory pathway. J. Biol. Chem. 274, 20745-20748.
    • (1999) J. Biol. Chem , vol.274 , pp. 20745-20748
    • Zhou, A.1    Webb, G.2    Zhu, X.3    Steiner, D.F.4
  • 16
    • 0032504250 scopus 로고    scopus 로고
    • Expression and characterization of a 70-kDa fragment of the insulin receptor that binds insulin. Minimizing ligand binding domain of the insulin receptor
    • Kristensen, C., Wiberg, F. C., Schaffer, L., and Andersen, A. S. (1998) Expression and characterization of a 70-kDa fragment of the insulin receptor that binds insulin. Minimizing ligand binding domain of the insulin receptor. J. Biol. Chem. 273, 17780-17786.
    • (1998) J. Biol. Chem , vol.273 , pp. 17780-17786
    • Kristensen, C.1    Wiberg, F.C.2    Schaffer, L.3    Andersen, A.S.4
  • 17
    • 20444411501 scopus 로고    scopus 로고
    • Characterization of the functional insulin binding epitopes of the full-length insulin receptor
    • Whittaker, J., and Whittaker, L. (2005) Characterization of the functional insulin binding epitopes of the full-length insulin receptor. J. Biol. Chem. 280, 20932-20936.
    • (2005) J. Biol. Chem , vol.280 , pp. 20932-20936
    • Whittaker, J.1    Whittaker, L.2
  • 20
    • 0027960567 scopus 로고
    • Cross-linking of a B25 azidophenylalanine insulin derivative to the carboxyl-terminal region of the alpha-subunit of the insulin receptor. Identification of a new insulin-binding domain in the insulin receptor
    • Kurose, T., Pashmforoush, M., Yoshimasa, Y., Carroll, R., Schwartz, G. P., Burke, G. T., Katsoyannis, P. G., and Steiner, D. F. (1994) Cross-linking of a B25 azidophenylalanine insulin derivative to the carboxyl-terminal region of the alpha-subunit of the insulin receptor. Identification of a new insulin-binding domain in the insulin receptor. J. Biol. Chem. 269, 29190-29197.
    • (1994) J. Biol. Chem , vol.269 , pp. 29190-29197
    • Kurose, T.1    Pashmforoush, M.2    Yoshimasa, Y.3    Carroll, R.4    Schwartz, G.P.5    Burke, G.T.6    Katsoyannis, P.G.7    Steiner, D.F.8
  • 21
    • 3142579218 scopus 로고    scopus 로고
    • Diabetes-associated mutations in insulin: Consecutive residues in the B chain contact distinct domains of the insulin receptor
    • Xu, B., Hu, S. Q., Chu, Y. C., Huang, K., Nakagawa, S. H., Whittaker, J., Katsoyannis, P. G., and Weiss, M. A. (2004) Diabetes-associated mutations in insulin: Consecutive residues in the B chain contact distinct domains of the insulin receptor. Biochemistry 43, 8356-8372.
    • (2004) Biochemistry , vol.43 , pp. 8356-8372
    • Xu, B.1    Hu, S.Q.2    Chu, Y.C.3    Huang, K.4    Nakagawa, S.H.5    Whittaker, J.6    Katsoyannis, P.G.7    Weiss, M.A.8
  • 22
    • 0027987462 scopus 로고
    • Transmembrane domain interactions are necessary for negative cooperativity of the insulin receptor
    • Whittaker, J., Garcia, P., Yu, G. Q., and Mynarcik, D. C. (1994) Transmembrane domain interactions are necessary for negative cooperativity of the insulin receptor. Mol. Endocrinol. 8, 1521-1527.
    • (1994) Mol. Endocrinol , vol.8 , pp. 1521-1527
    • Whittaker, J.1    Garcia, P.2    Yu, G.Q.3    Mynarcik, D.C.4
  • 23
    • 34247872895 scopus 로고    scopus 로고
    • Characterization of insulin/IGF hybrid receptors: Contributions of the insulin receptor L2 and Fn1 domains and the alternatively spliced exon 11 sequence to ligand binding and receptor activation
    • Benyoucef, S., Surinya, K. H., Hadaschik, D., and Siddle, K. (2007) Characterization of insulin/IGF hybrid receptors: contributions of the insulin receptor L2 and Fn1 domains and the alternatively spliced exon 11 sequence to ligand binding and receptor activation. Biochem. J. 403, 603-613.
    • (2007) Biochem. J , vol.403 , pp. 603-613
    • Benyoucef, S.1    Surinya, K.H.2    Hadaschik, D.3    Siddle, K.4
  • 24
    • 0035853774 scopus 로고    scopus 로고
    • Dimeric fragment of the insulin receptor alpha-subunit binds insulin with full holoreceptor affinity
    • Brandt, J., Andersen, A. S., and Kristensen, C. (2001) Dimeric fragment of the insulin receptor alpha-subunit binds insulin with full holoreceptor affinity. J. Biol. Chem. 276, 12378-12384.
    • (2001) J. Biol. Chem , vol.276 , pp. 12378-12384
    • Brandt, J.1    Andersen, A.S.2    Kristensen, C.3
  • 25
    • 0026795599 scopus 로고
    • Detection of a new hormone contact site within the insulin receptor ectodomain by the use of a novel photoreactive insulin
    • Fabry, M., Schaefer, E., Ellis, L., Kojro, E., Fahrenholz, F., and Brandenburg, D. (1992) Detection of a new hormone contact site within the insulin receptor ectodomain by the use of a novel photoreactive insulin. J. Biol. Chem. 267, 8950-8956.
    • (1992) J. Biol. Chem , vol.267 , pp. 8950-8956
    • Fabry, M.1    Schaefer, E.2    Ellis, L.3    Kojro, E.4    Fahrenholz, F.5    Brandenburg, D.6
  • 26
    • 33745763872 scopus 로고    scopus 로고
    • Characterization of a second ligand binding site of the insulin receptor
    • Hao, C., Whittaker, L., and Whittaker, J. (2006) Characterization of a second ligand binding site of the insulin receptor. Biochem. Biophys. Res. Commun. 347, 334-339.
    • (2006) Biochem. Biophys. Res. Commun , vol.347 , pp. 334-339
    • Hao, C.1    Whittaker, L.2    Whittaker, J.3
  • 27
    • 0027471973 scopus 로고
    • Signaling-competent receptor chimeras allow mapping of major insulin receptor binding domain determinants
    • Schumacher, R., Soos, M. A., Schlessinger, J., Brandenburg, D., Siddle, K., and Ullrich, A. (1993) Signaling-competent receptor chimeras allow mapping of major insulin receptor binding domain determinants. J. Biol. Chem. 268, 1087-1094.
    • (1993) J. Biol. Chem , vol.268 , pp. 1087-1094
    • Schumacher, R.1    Soos, M.A.2    Schlessinger, J.3    Brandenburg, D.4    Siddle, K.5    Ullrich, A.6
  • 28
    • 0026042468 scopus 로고
    • A region of the insulin receptor important for ligand binding (residues 450-601) is recognized by patients' autoimmune antibodies and inhibitory monoclonal antibodies
    • Zhang, B., and Roth, R. A. (1991) A region of the insulin receptor important for ligand binding (residues 450-601) is recognized by patients' autoimmune antibodies and inhibitory monoclonal antibodies. Proc. Natl. Acad. Sci. U.S.A. 88, 9858-9862.
    • (1991) Proc. Natl. Acad. Sci. U.S.A , vol.88 , pp. 9858-9862
    • Zhang, B.1    Roth, R.A.2
  • 30
    • 0032052278 scopus 로고    scopus 로고
    • An improved PCR-mutagenesis strategy for two-site mutagenesis or sequence swapping between related genes
    • Kirsch, R. D., and Joly, E. (1998) An improved PCR-mutagenesis strategy for two-site mutagenesis or sequence swapping between related genes. Nucleic Acids Res. 26, 1848-1850.
    • (1998) Nucleic Acids Res , vol.26 , pp. 1848-1850
    • Kirsch, R.D.1    Joly, E.2
  • 31
    • 0019826868 scopus 로고
    • Binding of insulin receptors to lectins: Evidence for common carbohydrate determinants on several membrane receptors
    • Hedo, J. A., Harrison, L. C., and Roth, J. (1981) Binding of insulin receptors to lectins: evidence for common carbohydrate determinants on several membrane receptors. Biochemistry 20, 3385-3393.
    • (1981) Biochemistry , vol.20 , pp. 3385-3393
    • Hedo, J.A.1    Harrison, L.C.2    Roth, J.3
  • 32
    • 0025281428 scopus 로고
    • Identification of epitopes on the human insulin receptor reacting with rabbit polyclonal antisera and mouse monoclonal antibodies
    • Prigent, S. A., Stanley, K. K., and Siddle, K. (1990) Identification of epitopes on the human insulin receptor reacting with rabbit polyclonal antisera and mouse monoclonal antibodies. J. Biol. Chem. 265, 9970-9977.
    • (1990) J. Biol. Chem , vol.265 , pp. 9970-9977
    • Prigent, S.A.1    Stanley, K.K.2    Siddle, K.3
  • 34
    • 0001314221 scopus 로고
    • The hemoglobin system. VI. The oxygen dissociation curve of hemoglobin
    • Adair, G. S. (1925) The hemoglobin system. VI. The oxygen dissociation curve of hemoglobin. J. Biol. Chem. 63, 529-545.
    • (1925) J. Biol. Chem , vol.63 , pp. 529-545
    • Adair, G.S.1
  • 37
    • 0026350498 scopus 로고
    • Systematic mutational analyses of protein-protein interfaces
    • Wells, J. A. (1991) Systematic mutational analyses of protein-protein interfaces. Methods Enzymol. 202, 390-411.
    • (1991) Methods Enzymol , vol.202 , pp. 390-411
    • Wells, J.A.1
  • 38
    • 0028980325 scopus 로고
    • Mapping of an NH2-terminal ligand binding site of the insulin receptor by alanine scanning mutagenesis
    • Williams, P. F., Mynarcik, D. C., Yu, G. Q., and Whittaker, J. (1995) Mapping of an NH2-terminal ligand binding site of the insulin receptor by alanine scanning mutagenesis. J. Biol. Chem. 270, 3012-3016.
    • (1995) J. Biol. Chem , vol.270 , pp. 3012-3016
    • Williams, P.F.1    Mynarcik, D.C.2    Yu, G.Q.3    Whittaker, J.4
  • 39
    • 0034637501 scopus 로고    scopus 로고
    • High affinity insulin binding by soluble insulin receptor extracellular domain fused to a leucine zipper
    • Hoyne, P. A., Cosgrove, L. J., McKern, N. M., Bentley, J. D., Ivancic, N., Elleman, T. C., and Ward, C. W. (2000) High affinity insulin binding by soluble insulin receptor extracellular domain fused to a leucine zipper. FEBS Lett. 479, 15-18.
    • (2000) FEBS Lett , vol.479 , pp. 15-18
    • Hoyne, P.A.1    Cosgrove, L.J.2    McKern, N.M.3    Bentley, J.D.4    Ivancic, N.5    Elleman, T.C.6    Ward, C.W.7
  • 40
    • 0029758766 scopus 로고    scopus 로고
    • Fusion of insulin receptor ectodomains to immunoglobulin constant domains reproduces high-affinity insulin binding in vitro
    • Bass, J., Kurose, T., Pashmforoush, M., and Steiner, D. F. (1996) Fusion of insulin receptor ectodomains to immunoglobulin constant domains reproduces high-affinity insulin binding in vitro. J. Biol. Chem. 271, 19367-19375.
    • (1996) J. Biol. Chem , vol.271 , pp. 19367-19375
    • Bass, J.1    Kurose, T.2    Pashmforoush, M.3    Steiner, D.F.4
  • 42
    • 0028268592 scopus 로고
    • A model for insulin binding to the insulin receptor
    • Schaffer, L. (1994) A model for insulin binding to the insulin receptor. Eur. J. Biochem. 221, 1127-1132.
    • (1994) Eur. J. Biochem , vol.221 , pp. 1127-1132
    • Schaffer, L.1
  • 43
    • 0032479179 scopus 로고    scopus 로고
    • Anatomy of hot spots in protein interfaces
    • Bogan, A. A., and Thorn, K. S. (1998) Anatomy of hot spots in protein interfaces. J. Mol. Biol. 280, 1-9.
    • (1998) J. Mol. Biol , vol.280 , pp. 1-9
    • Bogan, A.A.1    Thorn, K.S.2
  • 44
    • 0030050701 scopus 로고    scopus 로고
    • Binding in the growth hormone receptor complex
    • Wells, J. A. (1996) Binding in the growth hormone receptor complex. Proc. Natl. Acad. Sci U.S.A. 93, 1-6.
    • (1996) Proc. Natl. Acad. Sci U.S.A , vol.93 , pp. 1-6
    • Wells, J.A.1
  • 45
    • 10344238099 scopus 로고    scopus 로고
    • The high- and low-affinity receptor binding sites of growth hormone are allosterically coupled
    • Walsh, S. T., Sylvester, J. E., and Kossiakoff, A. A. (2004) The high- and low-affinity receptor binding sites of growth hormone are allosterically coupled. Proc. Natl. Acad. Sci. U.S.A. 101, 17078-17083.
    • (2004) Proc. Natl. Acad. Sci. U.S.A , vol.101 , pp. 17078-17083
    • Walsh, S.T.1    Sylvester, J.E.2    Kossiakoff, A.A.3
  • 46
    • 1542267773 scopus 로고    scopus 로고
    • Contributions of amino acid side chains to the kinetics and thermodynamics of the bivalent binding of protein L to Ig kappa light chain
    • Svensson, H. G., Wedemeyer, W. J., Ekstrom, J. L., Callender, D. R., Kortemme, T., Kim, D. E., Sjobring, U., and Baker, D. (2004) Contributions of amino acid side chains to the kinetics and thermodynamics of the bivalent binding of protein L to Ig kappa light chain. Biochemistry 43, 2445-2457.
    • (2004) Biochemistry , vol.43 , pp. 2445-2457
    • Svensson, H.G.1    Wedemeyer, W.J.2    Ekstrom, J.L.3    Callender, D.R.4    Kortemme, T.5    Kim, D.E.6    Sjobring, U.7    Baker, D.8
  • 47
    • 25144452720 scopus 로고    scopus 로고
    • Mutational analysis of the IFNAR1 binding site on IFNalpha2 reveals the architecture of a weak ligand-receptor binding-site
    • Roisman, L. C., Jaitin, D. A., Baker, D. P., and Schreiber, G. (2005) Mutational analysis of the IFNAR1 binding site on IFNalpha2 reveals the architecture of a weak ligand-receptor binding-site. J. Mol. Biol. 353, 271-281.
    • (2005) J. Mol. Biol , vol.353 , pp. 271-281
    • Roisman, L.C.1    Jaitin, D.A.2    Baker, D.P.3    Schreiber, G.4
  • 48
    • 48149095541 scopus 로고    scopus 로고
    • Alanine scanning of a putative receptor binding surface of insulin-like growth factor-I
    • Gauguin, L., Delaine, C., Alvino, C. L., McNeil, K. A., Wallace, J. C., Forbes, B. E., and De, M. P. (2008) Alanine scanning of a putative receptor binding surface of insulin-like growth factor-I. J. Biol. Chem. 283, 20821-20829.
    • (2008) J. Biol. Chem , vol.283 , pp. 20821-20829
    • Gauguin, L.1    Delaine, C.2    Alvino, C.L.3    McNeil, K.A.4    Wallace, J.C.5    Forbes, B.E.6    De, M.P.7
  • 49
    • 34250306385 scopus 로고    scopus 로고
    • Complementation analysis demonstrates that insulin cross-links both alpha subunits in a truncated insulin receptor dimer
    • Chan, S. J., Nakagawa, S., and Steiner, D. F. (2007) Complementation analysis demonstrates that insulin cross-links both alpha subunits in a truncated insulin receptor dimer. J. Biol. Chem. 282, 13754-13758.
    • (2007) J. Biol. Chem , vol.282 , pp. 13754-13758
    • Chan, S.J.1    Nakagawa, S.2    Steiner, D.F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.