224
Views
0
CrossRef citations to date
0
Altmetric
Research Articles

Prediction of a novel internal rearrangement of the insulin receptor

, , &
Pages 857-867 | Received 12 Aug 2015, Accepted 10 Mar 2016, Published online: 20 May 2016

References

  • Croll, T. I., Smith, B. J., Margetts, M. B., Whittaker, J. B., Weiss, M. A., Ward, C. W., & Lawrence, M. C. (2016). Higher-resolution structure of the human insulin receptor ectodomain: Multi-modal inclusion of the insert domain. Structure, 24, 469–476.
  • Denley, A., Cosgrove, L. J., Booker, G. W., Wallace, J. C., & Forbes, B. E. (2005). Molecular interactions of the IGF system. Cytokine and Growth Factor Reviews, 16, 421–439. doi:10.1016/j.cytogfr.2005.04.004
  • Deyev, I. E., Sohet, F., Vassilenko, K. P., Serova, O. V., Popova, N. V., Zozulya, S. A., … Petrenko, A. G. (2011). Insulin receptor-related receptor as an extracellular alkali sensor. Cell Metabolism, 13, 679–689. doi:10.1016/j.cmet.2011.03.022
  • Ebina, Y., Ellis, L., Jarnagin, K., Edery, M., Graf, L., Clauser, E., … Rutter, W. J. (1985). The human insulin receptor cDNA: The structural basis for hormone-activated transmembrane signalling. Cell, 40, 747–758. doi:10.1016/0092-8674(85)90334-4
  • Fan, J. R., Zheng, Q. C., Cui, Y. L., Li, W. K., & Zhang, H. X. (2015). Investigation of ligand selectivity in CYP3A7 by molecular dynamics simulations. Journal of Biomolecular Structure and Dynamics, 33, 2360–2367. doi:10.1080/07391102.2015.1054884
  • Ferguson, K. M., Berger, M. B., Mendrola, J. M., Cho, H. S., Leahy, D. J., & Lemmon, M. A. (2003). EGF activates its receptor by removing interactions that autoinhibit ectodomain dimerization. Molecular Cell, 11, 507–517. doi:10.1016/S1097-2765(03)00047-9
  • Florke, R. R., Schnaith, K., Passlack, W., Wichert, M., Kuehn, L., Fabry, M., … Reinauer, H. (2001). Hormone-triggered conformational changes within the insulin-receptor ectodomain: Requirement for transmembrane anchors. Biochemical Journal, 360, 189–198. doi:10.1042/bj3600189
  • Gracia, L. (2014). Clustering: Clustering tool. Retrieved from http://physiology.med.cornell.edu/faculty/hweinstein/vmdplugins/clustering/
  • Gupta, S., Jadaun, A., Kumar, H., Raj, U., Varadwaj, P. K., & Rao, A. R. (2015). Exploration of new drug-like inhibitors for serine/threonine protein phosphatase 5 of Plasmodium falciparum: a docking and simulation study. Journal of Biomolecular Structure and Dynamics, 33, 2421–2441. doi:10.1080/07391102.2015.1051114
  • Hess, B., Kutzner, C., van der Spoel, D., & Lindahl, E. (2008). GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation. Journal of Chemical Theory and Computation, 4, 435–447. doi:10.1021/ct700301q
  • Houde, D., & Demarest, S. J. (2011). Fine details of IGF-1R activation, inhibition, and asymmetry determined by associated hydrogen/deuterium-exchange and peptide mass mapping. Structure, 19, 890–900. doi:10.1016/j.str.2011.03.014
  • Humphrey, W., Dalke, A., & Schulten, K. (1996). VMD: Visual molecular dynamics. Journal of Molecular Graphics, 14, 33–38, 27–38. doi:10.1016/0263-7855(96)00018-5
  • Kalé, L., Skeel, R., Bhandarkar, M., Brunner, R., Gursoy, A., Krawetz, N., … Schulten, K. (1999). NAMD2: Greater scalability for parallel molecular dynamics. Journal of Computational Physics, 151, 283–312. doi:10.1006/jcph.1999.6201
  • Kara, I., Poggi, M., Bonardo, B., Govers, R., Landrier, J. F., Tian, S., … Peiretti, F. (2015). The paired basic amino acid-cleaving enzyme 4 (PACE4) is involved in the maturation of insulin receptor isoform B: An opportunity to reduce the specific insulin receptor-dependent effects of insulin-like growth factor 2 (IGF2). Journal of Biological Chemistry, 290, 2812–2821. doi:10.1074/jbc.M114.592543
  • Kavran, J. M., McCabe, J. M., Byrne, P. O., Connacher, M. K., Wang, Z., Ramek, A., … Leahy, D. J. (2014). How IGF-1 activates its receptor. eLife, 3, e03772. doi:10.7554/eLife.03772
  • Kristensen, C., Wiberg, F. C., Schaffer, L., & 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. Journal of Biological Chemistry, 273, 17780–17786. doi:10.1074/jbc.273.28.17780
  • Kristensen, C., Andersen, A. S., Ostergaard, S., Hansen, P. H., & Brandt, J. (2002). Functional reconstitution of insulin receptor binding site from non-binding receptor fragments. Journal of Biological Chemistry, 277, 18340–18345. doi:10.1074/jbc.M112249200
  • Lange, O. F., & Grubmuller, H. (2008). Full correlation analysis of conformational protein dynamics. Proteins, 70, 1294–1312. doi:10.1002/prot.21618
  • Longo, N., Langley, S. D., Griffin, L. D., & Elsas, L. J. (1993). Activation of glucose transport by a natural mutation in the human insulin receptor. Proceedings of the National Academy of Sciences, 90, 60–64. doi:10.1073/pnas.90.1.60
  • McKern, N. M., Lawrence, M. C., Streltsov, V. A., Lou, M. Z., Adams, T. E., Lovrecz, G. O., … Ward, C. W. (2006). Structure of the insulin receptor ectodomain reveals a folded-over conformation. Nature, 443, 218–221. doi:10.1038/nature05106
  • Menting, J. G., Whittaker, J., Margetts, M. B., Whittaker, L. J., Kong, G. K., Smith, B. J., … Lawrence, M. C. (2013). How insulin engages its primary binding site on the insulin receptor. Nature, 493, 241–245. doi:10.1038/nature11781
  • Menting, J. G., Yang, Y., Chan, S. J., Phillips, N. B., Smith, B. J., Whittaker, J., … Lawrence, M. C. (2014). Protective hinge in insulin opens to enable its receptor engagement. Proceedings of the National Academy of Sciences, 111, E3395–E3404. doi:10.1073/pnas.1412897111
  • Menting, J. G., Lawrence, C. F., Kong, G. K., Margetts, M. B., Ward, C. W., & Lawrence, M. C. (2015). Structural congruency of ligand binding to the insulin and insulin/type 1 insulin-like growth factor hybrid receptors. Structure, 23, 1271–1282. doi:10.1016/j.str.2015.04.016
  • Mynarcik, D. C., Williams, P. F., Schaffer, L., Yu, G. Q., & Whittaker, J. (1997). Analog binding properties of insulin receptor mutants. Identification of amino acids interacting with the COOH terminus of the B-chain of the insulin molecule. Journal of Biological Chemistry, 272, 2077–2081. doi:10.1074/jbc.272.4.2077
  • Ogiso, H., Ishitani, R., Nureki, O., Fukai, S., Yamanaka, M., Kim, J. H., … Yokoyama, S. (2002). Crystal structure of the complex of human epidermal growth factor and receptor extracellular domains. Cell, 110, 775–787. doi:10.1016/S0092-8674(02)00963-7
  • Pullen, R. A., Lindsay, D. G., Wood, S. P., Tickle, I. J., Blundell, T. L., Wollmer, A., … Gammeltoft, S. (1976). Receptor-binding region of insulin. Nature, 259, 369–373. doi:10.1038/259369a0
  • Qiang, G., Xue, S., Yang, J. J., Du, G., Pang, X., Li, X., … Ye, K. (2014). Identification of a small molecular insulin receptor agonist with potent antidiabetes activity. Diabetes, 63, 1394–1409. doi:10.2337/db13-0334
  • Renteria, M. E., Gandhi, N. S., Vinuesa, P., Helmerhorst, E., & Mancera, R. L. (2008). A comparative structural bioinformatics analysis of the insulin receptor family ectodomain based on phylogenetic information. PLoS One, 3, e3667. doi:10.1371/journal.pone.0003667
  • Schlitter, J., Engels, M., & Krüger, P. (1994). Targeted molecular dynamics: A new approach for searching pathways of conformational transitions. Journal of Molecular Graphics, 12, 84–89. doi:10.1016/0263-7855(94)80072-3
  • Smith, B. J., Huang, K., Kong, G., Chan, S. J., Nakagawa, S., Menting, J. G., … Lawrence, M. C. (2010). Structural resolution of a tandem hormone-binding element in the insulin receptor and its implications for design of peptide agonists. Proceedings of the National Academy of Sciences, 107, 6771–6776. doi:10.1073/pnas.1001813107
  • Trabuco, L. G., Villa, E., Mitra, K., Frank, J., & Schulten, K. (2008). Flexible fitting of atomic structures into electron microscopy maps using molecular dynamics. Structure, 16, 673–683. doi:10.1016/j.str.2008.03.005
  • Ullrich, A., Gray, A., Tam, A. W., Yang-Feng, T., Tsubokawa, M., Collins, C., … Chen, E. (1986). Insulin-like growth factor I receptor primary structure: comparison with insulin receptor suggests structural determinants that define functional specificity. EMBO Journal, 5, 2503–2512. doi:10.1371/journal.pone.0003667
  • Ward, C. W., & Lawrence, M. C. (2012). Similar but different: Ligand-induced activation of the insulin and epidermal growth factor receptor families. Current Opinion in Structural Biology, 22, 360–366. doi:10.1016/j.sbi.2012.03.014
  • Ward, C. W., Lawrence, M. C., Streltsov, V. A., Adams, T. E., & McKern, N. M. (2007). The insulin and EGF receptor structures: new insights into ligand-induced receptor activation. Trends in Biochemical Sciences, 32, 129–137. doi:10.1016/j.tibs.2007.01.001
  • Ward, C. W., Menting, J. G., & Lawrence, M. C. (2013). The insulin receptor changes conformation in unforeseen ways on ligand binding: Sharpening the picture of insulin receptor activation. BioEssays, 35, 945–954. doi:10.1002/bies201370111
  • Williams, P. F., Mynarcik, D. C., Yu, G. Q., & Whittaker, J. (1995). Mapping of an NH2-terminal ligand binding site of the insulin receptor by alanine scanning mutagenesis. Journal of Biological Chemistry, 270, 3012–3016. doi:10.1016/j.febslet.2004.03.077
  • Yang, L. Q., Sang, P., Tao, Y., Fu, Y. X., Zhang, K. Q., Xie, Y. H., & Liu, S. Q. (2014). Protein dynamics and motions in relation to their functions: several case studies and the underlying mechanisms. Journal of Biomolecular Structure and Dynamics, 32, 372–393. doi:10.1080/07391102.2013.770372

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.