The major theme of research in our laboratory focuses on biochemical, molecular, and structural studies on receptor-ligand recognition, protein-protein interaction, cell
signaling, and novel receptor/ligand discovery and engineering that are relevant to human chronic diseases such as diabetes,obesity, and inflammation. We are also interested in studying molecular recognition and signaling in host-pathogen interactions such as mechanisms of pathogen evasion of host immune defense.

Currently we have the following ongoing pilot projects:
(1) Structure and function studies of a newly discovered anti-obesity hormone, irisin.
(2) Molecular and structural basis of viral proteins counteracting host immune defense.
(3) How omega-3 fatty acids, such as DHA and EPA, the major ingredients in fish oil, bind to G protein-coupled receptor 120 (GPR120) and exert potent anti-inflammatory and anti-diabetic effects.
(4) Ligand binding and structural studies of a novel anti-inflammation drug target, lanthionine synthetase C-like 2 (collaborative project).

Xu B, Gewe M, Finton K, Strong RK. NK receptors. Encyclopedia of Signaling Molecules. Springer-Verlag Berlin Heidelberg 2012

Xu B, Pizarro JC, Holmes M, McBeth C, Groh V, Spies T, Strong RK. Crystal structure of a gamma-delta T cell receptor specific for human MHC class I homolog MICA. Proc Natl Acad Sci USA 2011, 108, 2414-2419.

Yang Y, Petkova A, Huang K, Xu B, Hua QX, Ye IJ, Chu YC, Hu SQ, Phillips NB, Whittaker J, Ismail-Beigi F, Mackin RB, Katsoyannis PG, Tycko R, Weiss MA. An Achilles' heel in an amyloidogenic protein and its repair: insulin fibrillation and therapeutic design. J. Biol. Chem. 2010, 285, 10806-10821.

Zhao M, Wan ZL, Whittaker L, Xu B, Phillips NB, Katsoyannis PG, Ismail-Beigi F, Whittaker J, Weiss MA. Design of an insulin analog with enhanced receptor-binding selectivity: rationale, structure, and therapeutic implications. J. Biol. Chem. 2009, 284, 32178-32187.

Xu B, Huang K, Chu YC, Hu SQ, Nakagawa S, Wang S, Wang R, Whittaker J, Katsoyannis PG, Weiss MA. Decoding the cryptic active conformation of a protein by synthetic photo-scanning. Insulin inserts a detachable arm between receptor domains. J. Biol. Chem. 2009, 284, 14597-14608.

Hua QX, Xu B, Huang K, Hu SQ, Nakagawa S, Jia WH, Wang S, Whittaker J, Katsoyannis PG, Weiss MA. Enhancing the activity of a protein by stereospecific unfolding. The conformational life cycle of insulin and its evolutionary origins. J. Biol. Chem. 2009, 284, 14586-14596.

Wan ZL, Huang K, Xu B, Hu SQ, Wang S, Chu YC, Katsoyannis PG, Weiss MA. Diabetes-associated mutations in human insulin: crystal structure and photo-cross-linking studies of a-chain variant insulin Wakayama. Biochemistry, 2005, 44: 5000-5016.

Wan ZL‡, Xu B‡, Huang K, Chu YC, Li B, Nakagawa SH, Qu Y, Hu SQ, Katsoyannis PG, Weiss MA. Enhancing the Activity of Insulin at the Receptor Interface: Crystal Structure and Photo-Cross-Linking of A8 Analogues. Biochemistry, 2004, 43: 16119-16133. ‡ Equal authorship.

Xu B., Hu S.Q., Chu Y.C., Wang S.H., Wang R.Y., Nakagawa S.H., Katsoyannis P.G., Weiss M.A. Diabetes-Associated Mutations in Human Insulin Identify Direct Hormone – Receptor Contacts. Diabetes. 2004, 53, 1599-1602.

Xu B, Hu SQ, Chu YC, Huang K, Nakagawa SH, Whittaker J, Katsoyannis PG, Weiss MA. Diabetes-associated mutations in insulin: consecutive residues in the B chain contact distinct domains of the insulin receptor. Biochemistry. 2004, 43, 8356-8372.