Xiang Chen, Ph.D.
Xiang Chen uses biophysical techniques to study how proteins are targeted for degradation. He has used NMR spectroscopy to solve the structures of the Rpn13:ubiquitin complex and of full-length hRpn13. The hRpn13 ubiquitin- and Uch37-binding domains interact, which weakens hRpn13 affinity for ubiquitin. Binding to the proteasome abrogates this interaction which, in turn, activates hRpn13 for ubiquitin. Xiang has also used NMR and mass spectroscopy to study how small molecules interact with hRpn13 to inhibit proteasome function.
Selected Key Publications
Structures of Rpn1 T1:Rad23UBL and hRpn13Pru:hLIC2UBL reveal distinct binding mechanisms between substrate receptors and shuttle factors of the proteasome.Structure. 24: 1257-1270, 2016. [ Journal Article ]
- Science. 351: In press, 2016. [ Journal Article ]
Structure of Proteasome Ubiquitin Receptor hRpn13 and its Activation by the Scaffolding Protein hRpn2.Mol Cell. 38: 404-415, 2010. [ Journal Article ]
- J Mol Biol. 392: 208-217, 2009. [ Journal Article ]
- Nature. 453: 548-552, 2008. [ Journal Article ]