Preliminary X-ray crystallographic studies of the TRAF domain of human TRAF4.

Abstract

TNF receptor-associated factor (TRAF) proteins were initially identified as tumour necrosis factor receptor (TNFR)-interacting proteins that perform critical functions in the regulation of inflammation, antiviral responses and apoptosis. Although TRAF4 is a canonical TRAF protein, it contains a unique domain boundary and functions differently in the cell. In this study, the human TRAF4 TRAF domain, corresponding to amino acids 290-470, was overexpressed in Escherichia coli using engineered C-terminal His tags. The TRAF4 TRAF domain was then purified to homogeneity and crystallized at 293 K. Finally, X-ray diffraction data were collected to a resolution of 2.3 Å from a crystal belonging to space group P2(1)2(1)2(1), with unit-cell parameters a = 58.9, b = 87.9, c = 117.3 Å, α = β = γ = 90°.

• Authors: Jong Hwan Yoon, Hyun Ho Park
• Journal: Acta crystallographica. Section F, Structural biology and crystallization communications (Acta Crystallogr Sect F Struct Biol Cryst Commun) Vol. 69 Issue Pt 9 Pg. 1026-8 (Sep 2013) ISSN: 1744-3091 [Electronic] England
• PMID: 23989155 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Recombinant Fusion Proteins
• TNF Receptor-Associated Factor 4
• TRAF4 protein, human

Topics

• Crystallography, X-Ray
• Escherichia coli (genetics)
• Gene Expression
• Humans
• Protein Structure, Tertiary
• Recombinant Fusion Proteins (chemistry, genetics, isolation & purification)
• TNF Receptor-Associated Factor 4 (chemistry, genetics, isolation & purification)