Expression, purification and preliminary crystallographic characterization of a novel segment from the neurofibromatosis type 1 protein

Acta Crystallogr D Biol Crystallogr. 2004 Dec;60(Pt 12 Pt 2):2364-7. doi: 10.1107/S0907444904026861. Epub 2004 Nov 26.

Abstract

Neurofibromin (MW 320 kDa) is the protein responsible for the pathogenesis of neurofibromatosis type 1 (NF1), one of the most common genetic diseases worldwide. The neurofibromin GAP-related domain (GRD, MW 38 kDa) possess a Ras-specific GTPase-activating protein property, which is at present its only clear biochemical function. This article describes the study of the bacterial production and preliminary X-ray crystallographic analysis of a neurofibromin fragment located at the C-terminal end of the GRD, which contains a region reported to be homologous to the yeast Sec14p lipid exchange protein. Of the three crystal variants obtained, a tetragonal form diffracted to a resolution of at least 2.3 A.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Animals
  • Cloning, Molecular
  • Crystallization
  • Crystallography, X-Ray
  • Drosophila / metabolism
  • Gene Deletion
  • Humans
  • Lipids / chemistry
  • Neurofibromin 1 / chemistry*
  • Phospholipid Transfer Proteins / chemistry
  • Protein Conformation
  • Protein Structure, Tertiary
  • Saccharomyces cerevisiae Proteins / chemistry

Substances

  • Lipids
  • Neurofibromin 1
  • Phospholipid Transfer Proteins
  • SEC14 protein, S cerevisiae
  • Saccharomyces cerevisiae Proteins