Expression, purification, crystallization and preliminary X-ray analysis of a truncated soluble domain of human glioma pathogenesis-related protein 1

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Nov 1;66(Pt 11):1487-9. doi: 10.1107/S1744309110035669. Epub 2010 Oct 28.

Abstract

Glioma pathogenesis-related protein 1 (GLIPR1) is a member of the CAP superfamily that includes proteins from a wide range of eukaryotic organisms. The biological functions of most CAP proteins, including GLIPR1, are unclear. GLIPR1 is up-regulated in aggressive glioblastomas and contributes to the invasiveness of cultured glioblastoma cells. In contrast, decreased GLIPR1 expression is associated with advanced prostate cancer. Forced GLIPR1 overexpression is pro-apoptotic in prostate cancer cells and is being tested in clinical trials as an experimental prostate-cancer therapy. Human GLIPR1 was expressed as a truncated soluble protein (sGLIPR1), purified and crystallized. Useful X-ray data have been collected to beyond 1.9 Å resolution from a crystal that belonged to the orthorhombic space group P2(1)2(1)2 with average unit-cell parameters a = 85.1, b = 79.5, c = 38.9 Å and either a monomer or dimer in the asymmetric unit.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Crystallization
  • Crystallography, X-Ray
  • Gene Expression
  • Humans
  • Neoplasm Proteins / chemistry*
  • Neoplasm Proteins / genetics
  • Neoplasm Proteins / isolation & purification
  • Nerve Tissue Proteins / chemistry*
  • Nerve Tissue Proteins / genetics
  • Nerve Tissue Proteins / isolation & purification
  • Solubility

Substances

  • GLIPR1 protein, human
  • Neoplasm Proteins
  • Nerve Tissue Proteins