作者: DEBORAH L. SEGALOFF , ROLF SPRENGEL , KAROLY NIKOLICS , MARIO ASCOLI
DOI: 10.1016/B978-0-12-571146-3.50014-6
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摘要: In summary, the LH/CG receptor is a single polypeptide which contains large hydrophilic domain that situated extracellularly, attached to region spans plasma membrane seven times, carboxy-terminal being intracellular. This topology was predicted by amino acid sequence and has been confirmed our immunofluorescence studies. The extracellular domain, related family of leucine-rich glycoproteins, presumably involved in binding glycoprotein hormones hCG LH. half receptor, rhodopsinlike receptors, (by analogy with these receptors) coupling G protein. Our transfection studies confirm this capable hormone activating adenylyl cyclase. Therefore, not only structure unique compared other cell surface receptors characterized date, but also its suggests mechanism translation protein different from protein-coupled whose ligands are much smaller intercalcate among transmembrane helices. We predict that, due homology hormones, structures FSH TSH share extensive structural receptor. Last, newly acquired knowledge about development cDNA antibodies for should enable more detailed on function regulation previously possible.