Crystal Structure of Reelin Repeats

  • Junichi Takagi

Reelin is a large glycoprotein with a repetitive modular structure (D’Arcangelo and Curran, 1999). It consists of a signal sequence, an F-spondin-like region, another region containing at least eight “reelin repeats,” and a C-terminal basic peptide of ∼30 residues (Fig. 5.1A). Each complete reelin repeat contains a central EGF module flanked by two subrepeats of 150–190 amino acids (Fig. 5.1A, inset). The central EGF module is relatively short in length (∼30 residues), but nevertheless has consensus signatures, including the spacings between cysteines (Campbell and Bork, 1993). Although the homology between subrepeat A and subrepeat B was first noted during the cloning of the reelin gene (D’Arcangelo et al., 1995), these repeats have failed to show any sequence homology to known protein domains.


Root Mean Square Concave Side Clostridium Thermocellum Reelin Gene Reelin Protein 
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  1. Bork, P., Downing, A. K., Kieffer, B., and Campbell, I. D. (1996). Structure and distribution of modules in extracellular proteins. Q. Rev. Biophys. 29:119-167.CrossRefPubMedGoogle Scholar
  2. Campbell, I. D., and Bork, P. (1993). Epidermal growth factor-like modules. Curr. Opin. Struct. Biol. 3:385-392.CrossRefGoogle Scholar
  3. Charnock, S. J., Bolam, D. N., Turkenburg, J. P., Gilbert, H. J., Ferreira, L. M., Davies, G. J., and Fontes, C. M. (2000). The X6 “thermostabilizing” domains of xylanases are carbohydrate-binding modules: structure and biochemistry of the Clostridium thermocellum X6b domain. Biochemistry 39:5013-5021.CrossRefPubMedGoogle Scholar
  4. Copley, R. R., Russell, R. B., and Ponting, C. P. (2001). Sialidase-like Asp-boxes: sequence-similar structures within different protein folds. Protein Sci. 10:285-292.CrossRefPubMedGoogle Scholar
  5. D’Arcangelo, G., and Curran, T. (1999). Reelin. In: Kreis, T., and Vale, R. (eds.), Guidebook to the Extracellular Matrix, Anchor, and Adhesion Receptors. Oxford University Press, Oxford, pp. 465-467.Google Scholar
  6. D’Arcangelo, G., Miao, G. G., Cheng, S. C., Soares, H. D., Morgen, J. I., and Curren, T. (1995). A protein related to extracellular matrix proteins mutant reeler. Nature 374: 719-723.CrossRefPubMedGoogle Scholar
  7. D’Arcangelo, G., Nakajima, K., Miyata, T., Ogawa, M., Mikoshiba, K., and Curran, T. (1997). Reelin is a secreted glycoprotein recognized by the CR-50 monoclonal antibody. J. Neurosci. 17:23-31.PubMedGoogle Scholar
  8. Ichihara, H., Jingami, H., and Toh, H. (2001). Three novel repetitive units of reelin. Brain Res. Mol. Brain Res. 97:190-193.CrossRefPubMedGoogle Scholar
  9. Iwasaki, K., Mitsuoka, K., Fujiyoshi, Y., Fujisawa, Y., Kikuchi, M., Sekiguchi, K., and Yamada, T. (2005). Electron tomography reveals diverse conformations of integrin alphaIIbbeta3 in the active state. J. Struct. Biol. 150:259-267.CrossRefPubMedGoogle Scholar
  10. Jossin, Y., Ignatova, N., Hiesberger, T., Herz, J., Lambert de Rouvroit, C., and Goffinet, A. M. (2004). The central fragment of reelin, generated by proteolytic processing in vivo, is critical to its function during cortical plate development. J. Neurosci. 24:514-521.CrossRefPubMedGoogle Scholar
  11. Kubo, K., Mikoshiba, K., and Nakajima, K. (2002). Secreted reelin molecules form homodimers. Neurosci. Res. 43:381-388.CrossRefPubMedGoogle Scholar
  12. Lugli, G., Krueger, J. M., Davis, J. M., Persico, A. M., Keller, F., and Smalheiser, N. R. (2003). Methodological factors influencing measurement and processing of plasma reelin in humans. BMC Biochem. 4:9.CrossRefPubMedGoogle Scholar
  13. Nogi, T., Yasui, N., Hattori, M., Iwasaki, K., and Takagi, J. (2006). Structure of a signaling-competent reelin fragment revealed by X-ray crystallography and electron tomography. EMBO J. 25:3675-3683.CrossRefPubMedGoogle Scholar
  14. Strasser, V., Fasching, D., Hauser, C., Mayer, H., Bock, H. H., Hiesberger, T., Herz, J., Weeber, E. J., Sweatt, J. D., Pramatarova, A., Howell, B., Schneider, W. J., and Nimpf, J. (2004). Receptor clustering is involved in reelin signaling. Mol. Cell Biol. 24:1378-1386.CrossRefPubMedGoogle Scholar
  15. Utsunomiya-Tate, N., Kubo, K., Tate, S., Kainosho, M., Katayama, E., Nakajima, K., and Mikoshiba, K. (2000). Reelin molecules assemble together to form a large protein complex, which is inhibited by the function-blocking CR-50 antibody. Proc. Natl. Acad. Sci. USA 97:9729-9734.CrossRefPubMedGoogle Scholar
  16. Weis, W. I., and Drickamer, K. (1996). Structural basis of lectin-carbohydrate recognition. Annu. Rev. Biochem. 65:441-473.CrossRefPubMedGoogle Scholar

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© Springer 2008

Authors and Affiliations

  • Junichi Takagi
    • 1
  1. 1.Laboratory of Protein Synthesis and Expression, Institute for Protein ResearchOsaka UniversityOsakaJapan

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