Material Discovery for TRAF6 Crystallization
- Others
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None
- *Abstract
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Tumour-necrosis factor (TNF) receptor-associated factor 6 (TRAF6), an important member of the TRAF family, is involved in the signal transduction of many pro-inflammatory receptors, such as CD40, IL-1 and IL-18 receptors, and the Toll-like receptors (including LPS receptors). Inhibiting TRAF6 signaling is therefore potentially beneficial for treating many autoimmune and inflammatory conditions. One way to achieve this is by inhibiting the direct interaction between TRAF6 and receptors. In this regard, it is highly advantageous to obtain high-resolution structural information on the interaction for rational drug design and optimization. The major obstacle for obtaining the structural information of TRAF6 has been the difficulty of identifying a crystallizable construct of TRAF6 for X-ray crystallography studies. Investigators at the Weill Medical College of Cornell University have succeeded in finding a crystallizable construct of TRAF6 for studying receptor interaction. The construct they obtained is small, easy to purify and easy to crystallize, representing an ideal fragment for obtaining structural information in drug design and optimization by both crystallography and NMR. The TRAF6 constructs can also be used for obtaining crystals of TRAF6 in complex with other binding partners. Nonexclusive use licenses are available.
- *Licensing
- Vibhu Sachdev(212) 746-6187sachdev@cornell.edu
- Country/Region
- USA
