Neuron
Volume 12, Issue 4, April 1994, Pages 717-731
Journal home page for Neuron

Article
Crystal structure of tandem type III fiibronectin domains from drosophila neuroglian at 2.0 å

https://doi.org/10.1016/0896-6273(94)90326-3Get rights and content

Abstract

We report the crystal structure of two adjacent fibronectin type III repeats from the Drosophila neural cell adhesion molecule neuroglian. Each domain consists of two antiparallel 0 sheets and is folded topologically identically to single fibronectin type III domains from the extracellular matrix proteins tenascin and fibronectin. β bulges and left-handed polyproline II helices disrupt the regular β sheet structure of both neuroglian domains. The hydrophobic interdomain interface includes a metalbinding site, presumably involved in stabilizing the relative orientation between domains and predicted by sequence comparision to be present in the vertebrate homolog molecule L1. The neuroglian domains are related by a near perfect 2-fold screw axis along the longest molecular dimension. Using this relationship, a model for arrays of tandem fibronectin type III repeats in neuroglian and other molecules is proposed.

References (55)

  • P.M. Snow et al.

    Fasciclin III: a novel homophilic adhesion molecule in Drosophila

    Cell

    (1989)
  • B.C. Wang

    Resolution of phase ambiguity in macromolecular crystallography

    Meth. Enzymol.

    (1985)
  • K.M. Yamada

    Adhesive recognition sequences

    J. Biol. Chem.

    (1991)
  • Y. Yoshihara et al.

    Immunoglobulin superfamily molecules in the nervous system

    Neurosci. Res.

    (1991)
  • F. Appel et al.

    Several extracellular domains of the neural cell adhesion molecule L1 are involved in neurite outgrowth and cell body adhesion

    J. Neurosci.

    (1993)
  • M. Baron et al.

    1H NMR assignment and secondary structure of the cell adhesion type III module of fibronectin

    Biochemistry

    (1992)
  • J.F. Bazan

    Structural design and molecular evolution of a cytokine receptor superfamily

  • P. Bork et al.

    Proposed acquisition of an animal protein domain by bacteria

  • R.L. Brady et al.

    Crystal structure of domains 3 and 4 of rat CD4: relation to the NHZ terminal domains

    Science

    (1993)
  • A.T. Brünger
  • A.T. Brünger

    Free R value: a novel statistical quantity for assessing the accuracy of crystal structures

    Nature

    (1992)
  • T.A. Bunch et al.

    Characterization and use of the Drosophila metallothionein promoter in cultured Drosophila melanogaster cells

    Nucl. Acids Res.

    (1988)
  • L. Cherbas et al.

    Cloning tissue culture cells

  • A.M. De Vos et al.

    Human Growth Hormone and Extracellular Domain of Its Receptor: Crystal Structure of the Complex

    Science

    (1992)
  • R.F. Doolittle

    Of URFS and ORFS: A Primer on How to Analyze Derived Amino Acid Sequences

    (1987)
  • T. Frei et al.

    Different extracellular domains of the neural cell adhesion molecule (N-CAM) are involved in different functions

    J. Cell Biol.

    (1992)
  • G. Grenningloh et al.

    Molecular genetics of neuronal recognition in Drosophila: evolution and function of the immunoglobulin superfamily cell adhesion molecules

  • Cited by (105)

    • Specific amino acids in the first fibronectin type III repeat of the neural cell adhesion molecule play a role in its recognition and polysialylation by the polysialyltransferase ST8Sia IV/PST

      2005, Journal of Biological Chemistry
      Citation Excerpt :

      NCAM has also been shown to interact with the prion protein, and both its FN1 and FN2 repeats are involved in this interaction (65). Numerous structural studies have demonstrated that although the Fn-III repeats of neural adhesion molecules do not exhibit significant sequence homology, they do share similar topology resembling that of an immunoglobulin constant domain (66–68). Each Fn-III repeat contains seven β-strands that are arranged in two antiparallel β-sheets consisting of three or four strands each (66–68).

    View all citing articles on Scopus
    View full text