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Research has been conducted on the gp130, a signal-transducing receptor for the four-helix cytokines family with the interleukin-6 as a prototypic member. Results indicate that the activation pathway of gp130 by LI-6-type cytokines can be dissected into separate sequential and cooperative activation complexes.

Tripeptide library screening and structure-guided methods, including fragment screening are used to find the improved peptide-based human beta tryptase inhibitors. The optimized compounds have exhibited low nanomolar potency against mast cell target with respect to serine protease off targets, thus the replacement of Lys/Arg at P1 in a peptide-like scaffold need not be accompanied by a loss in target affinity.

Studies the in vitro reconstitution of recognition and activation complexes between interleukin-6 and gp130, a shared signal-transducing receptor for cytokines. Extracellular activation pathway; Isolation of hetero-complexes by protein engineering strategy; Roles of the complexes in assembly of the active signaling oligomer.

( S)-3,4-Dicarboxyphenylglycine (DCPG) was first reported in 2001 as a potent orthosteric agonist with high subtype selectivity for the mGlu 8 receptor, but the structural basis for its high selectivity is not well understood. We have solved a cocrystal structure of recombinant human mGlu 8 amino terminal domain (ATD) protein bound to ( S)-DCPG, which possesses the largest lobe opening angle observed to date among known agonist-bound mGlu ATD crystal structures. The binding conformation of ( S)-DCPG observed in the crystal structure is significantly different from that in the homology model built from an l-glutamate-bound rat mGlu 1 ATD crystal structure, which has a smaller lobe opening angle. This highlights the importance of considering various lobe opening angles when modeling mGlu ATD-ligand complex. New homology models of other mGlu receptors based on the ( S)-DCPG-bound mGlu 8 ATD crystal structure were explored to rationalize ( S)-DCPG's high mGlu 8 receptor subtype selectivity.