Receptor-ligand binding specific

Elleman, T. C., Domagala, T., McKern, N. M., Nerrie, M., Lonnqvist, B., Adams, T. E., Lewis, J., Lovrecz, G. O., Hoyne, P. A., and Richards, K. M. et al. (2001). Identification of a determinant of epidermal growth factor receptor ligand-binding specificity using a truncated, high-affinity form of the ectodomain. Biochemistry 40, 8930-8939. 

IA (1997) Comparison of the ligand binding specificity and transcript tissue distribution of estrogen receptors a and (3. Endocrinol. 138, 863-70. 

ErbB (or HER in the human). There are four ErbB receptors that form homo- or heterodimers in various combinations upon ligand binding. Specific NRG isoforms preferentially interact with different ErbB dimers. The ErbB receptors are ligand-activated tyrosine kinases structurally similar to the EGF receptor. 

Figure 14-1. Signaling via G protein-coupled receptors. Ligand binding to its cell-surface receptor initiates interaction of the receptor with the heterotrimeric G protein for which it is specific. A conformational change in the G protein brought about by binding of the ligand-receptor complex promotes exchange of GDP for GTP. The activated Gd-GTP dissociates from the Gp complex and both can interact with effectors, which carry on the signal to the mechanism that implements the cellular response.

M. Kiriyama, F. Ushikubi, T. Kobayashi, M. Hirata, Y. Sugimoto, S. Nammiya, Ligand binding specificities of the eight types and subtypes of the mouse prostanoid receptors expressed in Chinese hamster ovary cells, Br. J. Pharmacol. 122 (1997) 217. 

Kobilka, B. K., Kobilka, T. S., Daniel, K., Regan, J. W., Caron, M. G., and Lefkowitz, R. J. (1988). Chimeric alpha 2-,beta 2-adrenergic receptors Delineation of domains involved in effector coupling and ligand binding specificity. Science 240, 1310-1316. 

Kuiper, G.G.J.M., Carlsson, B., Grandien, K., Enmark, E., Haggblad, J., Nilsson, S. and Gustafsson, J.A., Comparison of the ligand binding specificity and transcript tissue distribution of estrogen receptors alpha and beta, Endocrinology, 138, 863-870, 1997. 

Paas, Y, Eisenstein, M., Medevielle, F., Teichberg, V. I., and Devillers-Thiery, A. (1996). Identification of the amino acid subsets accounting for the ligand binding specificity of a glutamate receptor. Neuron 17, 979-990. 

Figure 3 Overview of the receptor-ligand binding process. All species involved are solvated by water (symbolized by gray spheres). The binding free energy difference between the bound and unbound state is a sum of enthalpic components (breaking and formation of hydrogen bonds, formation of specific hydrophobic contacts), and entropic components (release of water from hydrophobic surfaces to solvent, loss of conformational mobility of receptor and ligand).

---