title: 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.affiliation: School of Biotechnology and Graduate School of Biochemistry, Yeungnam University, Gyeungsan, Republic of Korea.
authors.forename: Jong Hwan
authors.initials: JH
authors.lastname: Yoon
authors.forename: Hyun Ho
authors.initials: HH
authors.lastname: Park
mesh_terms: D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000235:genetics; D015870:Gene Expression; D006801:Humans; D017434:Protein Structure, Tertiary; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification; D053449:TNF Receptor-Associated Factor 4 / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification
chemical_list: D011993:Recombinant Fusion Proteins; D053449:TNF Receptor-Associated Factor 4; C506367:TRAF4 protein, human
keywords: TRAF domain; TRAF4