메뉴 건너뛰기




Volumn 78, Issue 6, 2010, Pages 1531-1543

Erratum: Docking of insulin to a structurally equilibrated insulin receptor ectodomain (Originally Published in Proteins (2010) 78 (1531-1543) DOI: 10.1002/prot.22670);Dockina of insulin to a structurally equilibrated insulin receptor ectodomain

Author keywords

Conformational flexibility; Hormone recognition; Insulin receptor site 2; Molecular dynamics; Montecarlo docking; See saw mechanism

Indexed keywords

DIMER; DISULFIDE; EPITOPE; FIBRONECTIN; INSULIN; INSULIN RECEPTOR; PROTEIN TYROSINE KINASE; AMINO ACID; APOPROTEIN; MUTANT PROTEIN; PROTEIN SUBUNIT;

EID: 77951214213     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22740     Document Type: Erratum
Times cited : (19)

References (56)
  • 1
    • 0036782071 scopus 로고    scopus 로고
    • Structural biology of insulin and IGF1 receptors: Implications for drug design
    • DOI 10.1038/nrd917
    • De Meyts P, Whittaker J. Structural biology of insulin and IGF1 receptors: implications for drug design. Nat Rev Drug Discov 2002; 1: 769-783. (Pubitemid 37361561)
    • (2002) Nature Reviews Drug Discovery , vol.1 , Issue.10 , pp. 769-783
    • De Meyts, P.1    Whittaker, J.2
  • 2
    • 33847619358 scopus 로고    scopus 로고
    • The insulin and EGF receptor structures: New insights into ligandinduced receptor activation
    • Ward CW, Lawrence MC, Streltsov VA, Adams TE, McKern NM. The insulin and EGF receptor structures: new insights into ligandinduced receptor activation. Trends Biochem Sci 2007; 32: 129-137.
    • (2007) Trends Biochem Sci , vol.32 , pp. 129-137
    • Ward, C.W.1    Lawrence, M.C.2    Streltsov, V.A.3    Adams, T.E.4    McKern, N.M.5
  • 4
    • 36549015742 scopus 로고    scopus 로고
    • Insulin receptor structure and its implications for the IGF-1 receptor
    • DOI 10.1016/j.sbi.2007.07.007, PII S0959440X07001066, Catalysis and Regulation /Protein
    • Lawrence MC, McKern NM, Ward CW. Insulin receptor structure and its implications for the IGF-1 receptor. Curr Opin Struct Biol 2007; 17: 699-705. (Pubitemid 350180400)
    • (2007) Current Opinion in Structural Biology , vol.17 , Issue.6 , pp. 699-705
    • Lawrence, M.C.1    McKern, N.M.2    Ward, C.W.3
  • 6
    • 0021894451 scopus 로고
    • The nature and regulation of the insulin receptor: Structure and function
    • 6. Czech MP. The nature and regulation of the insulin receptor; structure and function. Annu Rev Physiol 1985; 47: 357-381. (Pubitemid 15142387)
    • (1985) Annual Review of Physiology , vol.47 , pp. 357-381
    • Czech, M.P.1
  • 8
    • 0015809277 scopus 로고
    • Insulin interactions with its receptors: Experimental evidence for negative coo-operativity
    • De Meyts P. Insulin interactions with its receptors: experimental evidence for negative coo-operativity. Biochem Biophys Res Commun 1973; 55: 154-161.
    • (1973) Biochem Biophys Res Commun , vol.55 , pp. 154-161
    • De Meyts, P.1
  • 9
    • 10844223660 scopus 로고    scopus 로고
    • Insulin and its receptor: Structure, function and evolution
    • DOI 10.1002/bies.20151
    • 9. De Meyts P. Insulin and its receptor: structure, function and evolution. BioEssays 2004; 26: 1351-1362. (Pubitemid 39664629)
    • (2004) BioEssays , vol.26 , Issue.12 , pp. 1351-1362
    • De Meyts, P.1
  • 10
    • 0028268592 scopus 로고
    • A model for insulin binding to the insulin receptor
    • Schäffer L. A model for insulin binding to the insulin receptor. Eur J Biochem 1994; 221: 1127-1132.
    • (1994) Eur J Biochem , vol.221 , pp. 1127-1132
    • Schäffer, L.1
  • 11
    • 0035890470 scopus 로고    scopus 로고
    • Hormone-triggered conformational changes within the insulin-receptor ectodomain: Requirement for transmembrane anchors
    • DOI 10.1042/0264-6021:3600189
    • Flörke RR, Schnaith K, Passlack W, Wiehert M, Kuehn L, Fabry M, Federwisch M, Reinauer H. Hormone-triggered conformational changes within the insulin-receptor ectodomain: requirement for transmembrane anchors. Biochem J 2001; 360: 189-198. (Pubitemid 33081964)
    • (2001) Biochemical Journal , vol.360 , Issue.1 , pp. 189-198
    • Florke, R.-R.1    Schnaith, K.2    Passlack, W.3    Wichert, M.4    Kuehn, L.5    Fabry, M.6    Federwisch, M.7    Reinauer, H.8
  • 12
    • 0028146822 scopus 로고
    • The structural basis of insulin and insulin-like growth factor-I receptor binding and negative co-operativity, and its relevance to mitogenic versus metabolic signalling
    • De Meyts P. The structural basis of insulin and insulin-like growth factor-I receptor binding and negative co-operativity, and its relevance to mitogenic versus metabolic signalling. Diabetologia 1994; 37(Suppl 2): S135-S148. (Pubitemid 24288803)
    • (1994) Diabetologia , vol.37 , Issue.SUPPL. 2
    • De Meyts, P.1
  • 14
    • 34250306385 scopus 로고    scopus 로고
    • Complementation analysis demonstrates that insulin cross-links both α subunits in a truncated insulin receptor dimer
    • DOI 10.1074/jbc.M700724200
    • Chan SJ, Nakagawa S, Steiner DF. Complementation analysis demonstrates that insulin cross-links both ct-subunits in a truncated insulin receptor dimer. J Biol Chem 2007; 282: 13754-13758. (Pubitemid 47100560)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.18 , pp. 13754-13758
    • Shu, J.C.1    Nakagawa, S.2    Steiner, D.F.3
  • 15
    • 60749092852 scopus 로고    scopus 로고
    • Harmonic oscillator model of the insulin and IGF1 receptors' allosteric binding and activation
    • Kiselyov W, Versteyhe S, Gauguin L, De Meyts P. Harmonic oscillator model of the insulin and IGF1 receptors' allosteric binding and activation. Mol Syst Biol. 2009; 5: 1-12.
    • (2009) Mol Syst Biol. , vol.5 , pp. 1-12
    • Kiselyov, W.1    Versteyhe, S.2    Gauguin, L.3    De Meyts, P.4
  • 16
    • 0028980325 scopus 로고
    • Mapping of an NH2-terminal ligand binding site of the insulin receptor by alanine scanning mutagenesis
    • Williams PF, Mynarcik DC, Yu GW, Whittaker J. Mapping of an NH2-terminal ligand binding site of the insulin receptor by alanine scanning mutagenesis. J Biol Chem 1995; 270: 3012-3016.
    • (1995) J Biol Chem , vol.270 , pp. 3012-3016
    • Williams, P.F.1    Mynarcik, D.C.2    Yu, G.W.3    Whittaker, J.4
  • 18
    • 0025350001 scopus 로고
    • Deletion analysis of the human insulin receptor ectodomain reveals independently folded soluble subdomains and insulin binding by a monomeric α-subunit
    • Schaefer EM, Siddle K, Ellis L. Deletion analysis of the human insulin receptor ectodomain reveals independently folded soluble subdomains and insulin binding by a monomeric ct-subunit. J Biol Chem 1990; 265: 13248-13253. (Pubitemid 20234279)
    • (1990) Journal of Biological Chemistry , vol.265 , Issue.22 , pp. 13248-13253
    • Schaefer, E.M.1    Siddle, K.2    Ellis, L.3
  • 19
    • 0028928843 scopus 로고
    • A single-chain insulin-like growth factor I/insulin hybrid binds with high affinity to the Insulin receptor
    • Kristensen C, Andersen AS, Hach M, Wiberg FC, Schärfer L, Kjeldsen T. A single-chain insulin-like growth factor I/insulin hybrid binds with high affinity to the Insulin receptor. Biochem J 1995; 305: 981-986.
    • (1995) Biochem J , vol.305 , pp. 981-986
    • Kristensen, C.1    Andersen, A.S.2    Hach, M.3    Wiberg, F.C.4    Schärfer, L.5    Kjeldsen, T.6
  • 21
    • 0035853774 scopus 로고    scopus 로고
    • Dimeric Fragment of the Insulin Receptor α-Subunit Binds Insulin with Full Holoreceptor Affinity
    • DOI 10.1074/jbc.M009402200
    • Brandt J, Andersen AS, Kristensen C. Dimeric fragment of the insulin receptor ct-subunit binds insulin with full holoreceptor affinity. J Biol Chem 2001; 276: 12378-12384. (Pubitemid 37385410)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.15 , pp. 12378-12384
    • Brandt, J.1    Andersen, A.S.2    Kristensen, C.3
  • 22
    • 0037053344 scopus 로고    scopus 로고
    • Role of insulin receptor dimerization domains in ligand binding, cooperativity, and modulation by anti-receptor antibodies
    • DOI 10.1074/jbc.M112014200
    • Surinya KH, Molina L, Soos MA, Brandt J, Kristensen. C, Siddle K. Role of insulin receptor dimerization domains in ligand binding, cooperativity, and modulation by anti-receptor antibodies. J Biol Chem 2002; 277: 16718-16725. (Pubitemid 34967692)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.19 , pp. 16718-16725
    • Surinya, K.H.1    Molina, L.2    Soos, M.A.3    Brandt, J.4    Kristensen, C.5    Siddle, K.6
  • 23
    • 0037166344 scopus 로고    scopus 로고
    • Functional reconstitution of insulin receptor binding site from nonbinding receptor fragments
    • Kristensen C, Andersen AS, Østergaard S, Hansen PH, Brandt J. Functional reconstitution of insulin receptor binding site from nonbinding receptor fragments, J Biol Chem 2002; 277: 18340-18345.
    • (2002) J Biol Chem , vol.277 , pp. 18340-18345
    • Kristensen, C.1    Andersen, A.S.2    Østergaard, S.3    Hansen, P.H.4    Brandt, J.5
  • 25
    • 0018102801 scopus 로고
    • Mapping of the residues responsible for the negative cooperativity of the receptor-binding region of insulin
    • De Meyts P, Obberghen EV, Roth J, Wollmer A, Brandenburg D. Mapping of the residues responsible for the negative cooperativity of the receptor-binding region of insulin. Nature 1978; 273: 504-509. (Pubitemid 8346576)
    • (1978) Nature , vol.273 , Issue.5663 , pp. 504-509
    • De Meyts, P.1    Van Obberghen, E.2    Roth, J.3
  • 27
    • 0034494052 scopus 로고    scopus 로고
    • Four new monomeric insulins obtained by alanine scanning the dimer-forming surface of the insulin molecule
    • Chen H, Shi M, Guo ZY, Tang YH, Qiao ZS, Liang ZH, Feng YM. Four new monomeric insulins obtained by alanine scanning the dimer-forming surface of the insulin molecule. Protein Eng 2000; 13: 779-782. (Pubitemid 32127576)
    • (2000) Protein Engineering , vol.13 , Issue.11 , pp. 779-782
    • Chen, H.1    Shi, M.2    Guo, Z.-Y.3    Tang, Y.-H.4    Qiao, Z.-S.5    Liang, Z.-H.6    Feng, Y.-M.7
  • 28
    • 0027960567 scopus 로고
    • Cross-linking of a B25 Azidophenylalanine insulin derivative to the carboxyl-terminal regions of the ct-subunit of the insulin receptor
    • Kurose T, Pashmforoush M, Yoshimasa Y, Carroll R, Schwartz GP, Burke GT, Katsoyannis PG, Steiner DF. Cross-linking of a B25 Azidophenylalanine insulin derivative to the carboxyl-terminal regions of the ct-subunit of the insulin receptor. J Biol Chem 1994; 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
  • 29
    • 13344279398 scopus 로고    scopus 로고
    • Alanine-scanning mutagenesis of a C-terminal ligand binding domain of the insulin receptor α subunit
    • DOI 10.1074/jbc.271.5.2439
    • Mynarcik DC, Yu GQ, Whittaker J. Alanine-scanning mutagenesis of a C-terminal ligand binding domain in the insulin receptor a subunit. J Biol Chem 1996; 271: 2439-2442. (Pubitemid 26047846)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.5 , pp. 2439-2442
    • Mynarcik, D.C.1    Yu, G.Q.2    Whittaker, J.3
  • 30
    • 0033601260 scopus 로고    scopus 로고
    • Specificity of insulin and insulin-like growth factor i receptors investigated using chimeric mini-receptors
    • Kristensen C, Wiberg FC, Andersen AS. Specificity of insulin and insulin-like growth factor I receptors investigated using chimeric mini-receptors. J Biol Chem 1999; 274: 37351-37356.
    • (1999) J Biol Chem , vol.274 , pp. 37351-37356
    • Kristensen, C.1    Wiberg, F.C.2    Andersen, A.S.3
  • 31
    • 0033972485 scopus 로고    scopus 로고
    • Structural domains of the insulin receptor and IGF receptor required for dimerisation and ligand binding
    • DOI 10.1016/S0014-5793(00)01161-3, PII S0014579300011613
    • Molina L, Marino-Busije C, Quinn DR, Siddle K. Structural domains of the insulin receptor and IGF receptor required for dimerization and. ligand binding. FEBS Lett 2000; 467: 226-230. (Pubitemid 30081739)
    • (2000) FEBS Letters , vol.467 , Issue.2-3 , pp. 226-230
    • Molina, L.1    Marino-Buslje, C.2    Quinn, D.R.3    Siddle, K.4
  • 32
    • 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, Roth RA. 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 USA 1991; 88: 9858-9862. (Pubitemid 21915733)
    • (1991) Proceedings of the National Academy of Sciences of the United States of America , vol.88 , Issue.21 , pp. 9858-9862
    • Zhang, B.1    Roth, R.A.2
  • 33
    • 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, Brandenburg D. Detection of a new hormone contact site within the insulin receptor ectodomain by the use of a novel photoreactive insulin. J Biol Chem 1992; 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
  • 35
    • 33745763872 scopus 로고    scopus 로고
    • Characterization of a second ligand binding site of the insulin receptor
    • DOI 10.1016/j.bbrc.2006.06.089, PII S0006291X06014021
    • Hao C, Whittaker L, Whittaker J. Characterization of a second ligand binding site of the insulin receptor. Biochem Biophys Res Commun 2006; 347: 334: 339. (Pubitemid 44015681)
    • (2006) Biochemical and Biophysical Research Communications , vol.347 , Issue.1 , pp. 334-339
    • Hao, C.1    Whittaker, L.2    Whittaker, J.3
  • 36
    • 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
    • DOI 10.1042/BJ20061709
    • Benyoucef S, Surinya KH, Hadaschik D, Siddle K. Characterization of insulin/IGF hybrid receptors: contributions of the insulin receptor L2 and Fn1 domains and the alternatively spliced exou 11 sequence to ligand binding and receptor activation. Biochem J 2007; 403: 603-613. (Pubitemid 46706989)
    • (2007) Biochemical Journal , vol.403 , Issue.3 , pp. 603-613
    • Benyoucef, S.1    Surinya, K.H.2    Hadaschik, D.3    Siddle, K.4
  • 37
    • 57049086436 scopus 로고    scopus 로고
    • High-affinity insulin binding: Insulin interacts with two receptor ligand binding sites
    • Whittaker L, Hao C, Fu W, Whittaker J. High-affinity insulin binding: insulin interacts with two receptor ligand binding sites. Biochemistry 2008; 47: 12900-12909.
    • (2008) Biochemistry , vol.47 , pp. 12900-12909
    • Whittaker, L.1    Hao, C.2    Fu, W.3    Whittaker, J.4
  • 38
    • 3142579218 scopus 로고    scopus 로고
    • Diabetes-associated mutations in insulin: Consecutive residues in the B chain contact distinct domains of the insulin receptor
    • DOI 10.1021/bi0497796
    • Xu B, Hu SQ, Chu YC, Huang K, Nakagawa SH, Katsoyannis PG, Weiss MA. Diabetes-associated mutations in insulin: consecutive residues in the B chain contact distinct domains of the insulin receptor. Biochemistry 2004; 43: 8356-8372. (Pubitemid 38902515)
    • (2004) Biochemistry , vol.43 , Issue.26 , 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
  • 44
    • 3142714765 scopus 로고    scopus 로고
    • Extending the treatment of backbone energetics in protein force fields: Limitations of gasphase quantum mechanics in reproducing protein conformational distributions in molecular dynamics simulations
    • MacKerell AD, Jr., Feig M, Brooks CL, III., Extending the treatment of backbone energetics in protein force fields: limitations of gasphase quantum mechanics in reproducing protein conformational distributions in molecular dynamics simulations. J Comput Chem 2004; 25: 1400-1415.
    • (2004) J Comput Chem , vol.25 , pp. 1400-1415
    • MacKerell Jr., A.D.1    Feig, M.2    Brooks III, C.L.3
  • 47
    • 0022879089 scopus 로고
    • Role of the phenylalanine B25 side chain in directing insulin inter-action with its receptor
    • Nakagawa SH, Tager HS. Role of the phenylalanine B25 side chain in directing insulin inter-action with its receptor. J Biol Chem 1986; 261: 7332-7341.
    • (1986) J Biol Chem , vol.261 , pp. 7332-7341
    • Nakagawa, S.H.1    Tager, H.S.2
  • 49
    • 0022474285 scopus 로고
    • Monoclonal antibodies reacting with multiple epitopes on the human insulin receptor
    • Soos MA, Siddle K, Baron MD, Heward JM, Luzio JP, Bellatin J, Lennox ES. Monoclonal antibodies reacting with multiple epitopes on the human insulin receptor. Biochem J 1986; 235: 199-208. (Pubitemid 16041992)
    • (1986) Biochemical Journal , vol.235 , Issue.1 , pp. 199-208
    • Soos, M.A.1    Siddle, K.2    Baron, M.D.3
  • 50
    • 0027987462 scopus 로고
    • Transmembrane domain interactions are necessary for negative cooperativity of the insulin-receptor
    • Whittaker J, Garcia P, Yu GQ, Mynarcik DC. Transmembrane domain interactions are necessary for negative cooperativity of the insulin-receptor. Mol Endocrinol 1994; 8: 1521-1526.
    • (1994) Mol Endocrinol , vol.8 , pp. 1521-1526
    • Whittaker, J.1    Garcia, P.2    Yu, G.Q.3    Mynarcik, D.C.4
  • 52
    • 16344376210 scopus 로고    scopus 로고
    • Chiral mutagenesis of insulin. Foldability and function are inversely regulated by a stereospecific switch in the B chain
    • Nakagawa SH, Zhao M, Hua QX, Hu SQ, Wan ZL, Jia W, Weiss MA. Chiral mutagenesis of insulin. Foldability and function are inversely regulated by a stereospecific switch in the B chain. Biochemistry 2005; 44: 4984-4999.
    • (2005) Biochemistry , vol.44 , pp. 4984-4999
    • Nakagawa, S.H.1    Zhao, M.2    Hua, Q.X.3    Hu, S.Q.4    Wan, Z.L.5    Jia, W.6    Ma, W.7
  • 53
    • 56349123217 scopus 로고    scopus 로고
    • A comparative structural bioinformatics analysis of the insulin receptor family ectodomain based on phylogenetic information
    • Renteria ME, Gandhi HS, Vinuesa P, Helmerhorst E, Mancera RL. A comparative structural bioinformatics analysis of the insulin receptor family ectodomain based on phylogenetic information. PLoS ONE 2008; 3: e3667.
    • (2008) PLoS ONE , vol.3
    • Renteria, M.E.1    Gandhi, H.S.2    Vinuesa, P.3    Helmerhorst, E.4    Mancera, R.L.5
  • 54
    • 48149095486 scopus 로고    scopus 로고
    • The insulin receptor: A prototype for dimeric, allosteric membrane receptors?
    • De Meyts P. The insulin receptor: a prototype for dimeric, allosteric membrane receptors? Trends Biochem Sci 2008; 33: 376-384.
    • (2008) Trends Biochem Sci , vol.33 , pp. 376-384
    • De Meyts, P.1
  • 55
    • 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
    • DOI 10.1074/jbc.M704599200
    • 55. Jensen M, Hansen B, De Meyts P, Schaeffer L, Urso B. Activation of the insulin receptor by insulin and a synthetic peptide leads to divergent metabolic and mitogenic signaling and responses. J Biol Chem 2007; 282: 35179-35186. (Pubitemid 350232483)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.48 , pp. 35179-35186
    • Jensen, M.1    Hansen, B.2    De Meyts, P.3    Schaffer, L.4    Urso, B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.