A molecular dissection of the glycoprotein hormone receptors.

@article{citeulike:702189, abstract = {In glycoprotein hormone receptors, a subfamily of rhodopsin-like G protein-coupled receptors, the recognition and activation steps are carried out by separate domains of the proteins. Specificity of recognition of the hormones thyrotropin (TSH), lutropin (LH), human chorionic gonadotropin (hCG) and follitropin (FSH) involves leucine-rich repeats (LRRs) present in an N-terminal ectodomain, and can be associated with a limited number of residues at key positions of the LRRs. The mechanism by which binding of the hormones results in activation is proposed to involve switching of the ectodomain from a tethered inverse agonist to a full agonist of the serpentine, rhodopsin-like region of the receptor. Unexpectedly, the picture is complicated by the observation that promiscuous activation of one of the receptors (FSHr) by hCG or TSH can result from activating mutations affecting the serpentine region of the receptors.}, address = {IRIBHM, Universit\'{e} Libre de Bruxelles, B-1070, Brussels, Belgium. gvassart@ulb.ac.be}, author = {Vassart, G. and Pardo, L. and Costagliola, S. }, citeulike-article-id = {702189}, doi = {http://dx.doi.org/10.1016/j.tibs.2004.01.006}, issn = {0968-0004}, journal = {Trends Biochem Sci}, keywords = {gpcr, hormone, structure, thyrotropin}, month = {March}, number = {3}, pages = {119--126}, posted-at = {2006-06-20 12:16:16}, priority = {2}, title = {A molecular dissection of the glycoprotein hormone receptors.}, url = {http://dx.doi.org/10.1016/j.tibs.2004.01.006}, volume = {29}, year = {2004} }

TY - JOUR ID - citeulike:702189 L3 - citeulike-article-id:702189 N2 - In glycoprotein hormone receptors, a subfamily of rhodopsin-like G protein-coupled receptors, the recognition and activation steps are carried out by separate domains of the proteins. Specificity of recognition of the hormones thyrotropin (TSH), lutropin (LH), human chorionic gonadotropin (hCG) and follitropin (FSH) involves leucine-rich repeats (LRRs) present in an N-terminal ectodomain, and can be associated with a limited number of residues at key positions of the LRRs. The mechanism by which binding of the hormones results in activation is proposed to involve switching of the ectodomain from a tethered inverse agonist to a full agonist of the serpentine, rhodopsin-like region of the receptor. Unexpectedly, the picture is complicated by the observation that promiscuous activation of one of the receptors (FSHr) by hCG or TSH can result from activating mutations affecting the serpentine region of the receptors. IS - 3 JF - Trends Biochem Sci SN - 0968-0004 AD - IRIBHM, Université Libre de Bruxelles, B-1070, Brussels, Belgium. gvassart@ulb.ac.be EP - 126 TI - A molecular dissection of the glycoprotein hormone receptors. VL - 29 SP - 119 KW - gpcr KW - hormone KW - structure KW - thyrotropin AU - Vassart, G AU - Pardo, L AU - Costagliola, S PY - 2004/03// UR - http://dx.doi.org/10.1016/j.tibs.2004.01.006 ER -