Crystallization and preliminary X-ray analysis of the TRAF domain of TRAF3

Acta Crystallogr D Biol Crystallogr. 2002 Aug;58(Pt 8):1340-2. doi: 10.1107/s0907444902008958. Epub 2002 Jul 20.

Abstract

Tumor necrosis factor receptors (TNFR) signal events in immune responses, Ig class switching, activation of NF-kappaB or regulation of apoptosis. TNFR-associated factors (TRAFs) are adaptor proteins that connect TNFRs to downstream signaling pathways, including the NF-kappaB and c-JUN N-terminal kinase (JNK) pathways. Members of the TRAF family exist as trimers and share a conserved TRAF domain that mediates binding to the cytoplasmic domains of TNFRs. The TRAF domain from TRAF3 has been crystallized. In addition, an N-terminally truncated form of the domain has been crystallized in space group P321 with a shortened c axis and markedly improved diffraction (2.5 A resolution).

Publication types

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

MeSH terms

  • Crystallization
  • Crystallography, X-Ray
  • Humans
  • Molecular Structure
  • Protein Structure, Tertiary
  • Proteins / chemistry*
  • Recombinant Proteins / chemistry
  • TNF Receptor-Associated Factor 3

Substances

  • Proteins
  • Recombinant Proteins
  • TNF Receptor-Associated Factor 3