Crystallization and preliminary crystallographic studies of CCM3 in complex with the C-terminal domain of MST4

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Jul 1;68(Pt 7):760-3. doi: 10.1107/S1744309112016843. Epub 2012 Jun 27.

Abstract

MST4 is a member of the GCKIII kinases. The interaction between cerebral cavernous malformation 3 (CCM3) and GCKIII kinases plays a critical role in cardiovascular development and in cerebral cavernous malformations. The complex of CCM3 and the C-terminal domain of MST4 has been constructed, purified and crystallized, and a diffraction data set has been collected to 2.4 Å resolution. The crystal of the CCM3-MST4 C-terminal domain complex belonged to space group P4(1)2(1)2 or P4(3)2(1)2, with unit-cell parameters a = 69.10, b = 69.10, c = 117.57 Å.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Apoptosis Regulatory Proteins / chemistry*
  • Apoptosis Regulatory Proteins / metabolism
  • Crystallization
  • Crystallography, X-Ray
  • Humans
  • Membrane Proteins / chemistry*
  • Membrane Proteins / metabolism
  • Protein Binding
  • Protein Serine-Threonine Kinases / chemistry*
  • Protein Serine-Threonine Kinases / metabolism
  • Proto-Oncogene Proteins / chemistry*
  • Proto-Oncogene Proteins / metabolism

Substances

  • Apoptosis Regulatory Proteins
  • Membrane Proteins
  • PDCD10 protein, human
  • Proto-Oncogene Proteins
  • STK26 protein, human
  • Protein Serine-Threonine Kinases