Receptor interface

Pearce, K.H., Jr., M.H. Ultsch, R.F. Kelley, A.M. de Vos, and J.A. Wells. 1996. Structural and mutational analysis of affinity-inert contact residues at the growth hormone-receptor interface. Biochemistry 35 10300-10307. 

Clackson T., Wells J.A. A hot spot of binding energy in a hormone-receptor interface. Science 1995, 267, 383-386. 

Verkhivker GM, Bouzida D, Gehlhaar DK, Rejto PA, Freer ST, Rose PM(2003) Computational detection of the binding-site hot spot at the remodelled human growth hormone-receptor interface, Proteins, 53 201-219... 

Clackson T, Wells JA (1995) A hot spot of binding energy hormone-receptor interfaces, Science, 267 383-386... 

T. Clackson and J.A. Wells, (1995). A Hot Spot of Binding Energy in a Hormone-Receptor Interface. Science 267, 383-386. 

Structure correlation to map reaction pathways might become important in the field of the monoclonal catalytic antibodies [145, 146]. These proteins are produced by the immune system to bind molecules which resemble the transition state of a chemical reaction. They show catalytic properties with high substrate specificity. Reactions can be imagined for which a biochemical catalyst is not yet known (e.g. the Diels-Alder reaction). The rational design of catalysts for these reactions requires detailed information about possible transition-state structures, geometrical and energetic aspects of the ligand/receptor interface and results from structure/reactivity relationships which are available from structure correlation. 

J.T. Koh, Engineering selectivity and discrimination into ligand-receptor interfaces, Chem. Biol. 2002, 9(1), 17-23. 

ERs (Fig. 3.3-6(b)). This greater selectivity is imparted as a result of weaker binding of the carboxylate-functionalized ligands to the wild type, presumably as a result of mismatched polar interactions at the ligand-receptor interface. 

---