Expression, purification, crystallization and preliminary X-ray crystallographic analysis of the extracellular olfactomedin domain of gliomedin

Acta Crystallogr F Struct Biol Commun. 2014 Nov;70(Pt 11):1536-9. doi: 10.1107/S2053230X14020305. Epub 2014 Oct 25.

Abstract

Gliomedin (GLDN) is one of the essential proteins in the development of the nodes of Ranvier in the vertebrate peripheral nervous system. An olfactomedin (OLF) domain is located at the GLDN extracellular C-terminus and is involved in the accumulation of neuronal plasma membrane voltage-gated sodium channels in the nodes by interacting with neurofascin and NrCAM. No structures of OLF domains have previously been reported. Here, the crystallization of the rat GLDN OLF domain, which was expressed in an insect-cell system, is reported. The crystal diffracted to 1.55 Å resolution and belonged to space group P2₁, with unit-cell parameters a=37.5, b=141.7, c=46.0 Å, β=110.6°, and had two molecules in the asymmetric unit.

Keywords: Schwann cell; cell adhesion; gliomedin; myelin; olfactomedin.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cell Adhesion Molecules, Neuronal / biosynthesis*
  • Cell Adhesion Molecules, Neuronal / chemistry*
  • Cell Adhesion Molecules, Neuronal / isolation & purification
  • Cell Line
  • Crystallization
  • Crystallography, X-Ray
  • Extracellular Matrix Proteins / biosynthesis*
  • Extracellular Matrix Proteins / chemistry*
  • Extracellular Matrix Proteins / isolation & purification
  • Gene Expression Regulation
  • Glycoproteins / biosynthesis*
  • Glycoproteins / chemistry*
  • Glycoproteins / isolation & purification
  • Insecta
  • Molecular Sequence Data
  • Protein Structure, Tertiary / physiology
  • Rats

Substances

  • Cell Adhesion Molecules, Neuronal
  • Extracellular Matrix Proteins
  • Glycoproteins
  • gliomedin, rat
  • olfactomedin