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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, ? = ? = ? = 90°.

SUBMITTER: Yoon JH

PROVIDER: S-EPMC3758155 | biostudies-literature | 2013 Sep

REPOSITORIES: biostudies-literature

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

Yoon Jong Hwan JH Park Hyun Ho HH

Acta crystallographica. Section F, Structural biology and crystallization communications 20130821 Pt 9

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-ter ...[more]

PMID: 23989155

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