Crystallization and preliminary crystallographic analysis of the importin-beta-SREBP-2 complex

Acta Crystallogr D Biol Crystallogr. 2003 Oct;59(Pt 10):1866-8. doi: 10.1107/s0907444903018328. Epub 2003 Sep 19.

Abstract

The nuclear-transport protein importin-beta mediates the nuclear import of the transcription factor SREBP-2 without requiring adaptor proteins such as importin-alpha. An importin-beta-SREBP-2 HLHZ domain complex was purified and crystallized. The crystals belong to space group P2(1)2(1)2(1) and show diffraction to at least 3.0 A resolution. The unit-cell parameters are a = 101.0, b = 113.2, c = 240.0 A. Structure determination using the MAD or SAD method is under way.

MeSH terms

  • Animals
  • Crystallization
  • Crystallography, X-Ray / methods
  • DNA-Binding Proteins / biosynthesis
  • DNA-Binding Proteins / chemistry*
  • DNA-Binding Proteins / genetics
  • Humans
  • Mice
  • Protein Structure, Tertiary
  • Recombinant Proteins / biosynthesis
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Sterol Regulatory Element Binding Protein 2
  • Transcription Factors / biosynthesis
  • Transcription Factors / chemistry*
  • Transcription Factors / genetics
  • beta Karyopherins / biosynthesis
  • beta Karyopherins / chemistry*
  • beta Karyopherins / genetics

Substances

  • DNA-Binding Proteins
  • Recombinant Proteins
  • SREBF2 protein, human
  • Srebf2 protein, mouse
  • Sterol Regulatory Element Binding Protein 2
  • Transcription Factors
  • beta Karyopherins