Expression, crystallization and preliminary X-ray analysis of extracellular modules of the neural cell-adhesion molecules NCAM and L1

Acta Crystallogr D Biol Crystallogr. 2004 Mar;60(Pt 3):591-3. doi: 10.1107/S0907444904001167. Epub 2004 Feb 25.

Abstract

Recombinant proteins consisting of either the four or five amino-terminal immunoglobulin (Ig) modules of the rat neural cell-adhesion molecule NCAM or the whole extracellular part [six Ig and five fibronectin type III (F3) modules] of mouse L1 have been expressed in Drosophila S2 cells. The proteins have been purified and crystallized. The crystals of the recombinant protein containing the four amino-terminal Ig modules of NCAM diffract X-rays to approximately 4 A resolution and belong to space group P622 or P6(3)22, with unit-cell parameters a = b = 258.7, c = 182.4 A. No diffraction was observed for the other two protein constructs. This is a step towards determining the structure of multimodular constructs of cell-adhesion molecules that exhibit high structural flexibility.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cell Line
  • Crystallization
  • Crystallography, X-Ray
  • Drosophila / cytology
  • Drosophila / genetics
  • Gene Expression
  • Mice
  • Neural Cell Adhesion Molecule L1 / chemistry*
  • Neural Cell Adhesion Molecule L1 / genetics
  • Protein Structure, Tertiary / genetics
  • Rats
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics

Substances

  • Neural Cell Adhesion Molecule L1
  • Recombinant Proteins