PubMed:7984244 JSONTXT

{"project":"AIMed","denotations":[{"id":"T1","span":{"begin":25,"end":39},"obj":"protein"},{"id":"T2","span":{"begin":40,"end":49},"obj":"protein"},{"id":"T3","span":{"begin":98,"end":112},"obj":"protein"},{"id":"T4","span":{"begin":114,"end":117},"obj":"protein"},{"id":"T5","span":{"begin":123,"end":132},"obj":"protein"},{"id":"T6","span":{"begin":134,"end":138},"obj":"protein"},{"id":"T7","span":{"begin":353,"end":356},"obj":"protein"},{"id":"T8","span":{"begin":361,"end":365},"obj":"protein"},{"id":"T9","span":{"begin":377,"end":381},"obj":"protein"},{"id":"T10","span":{"begin":386,"end":391},"obj":"protein"},{"id":"T11","span":{"begin":796,"end":799},"obj":"protein"},{"id":"T12","span":{"begin":1028,"end":1032},"obj":"protein"},{"id":"T13","span":{"begin":1054,"end":1057},"obj":"protein"},{"id":"T14","span":{"begin":1072,"end":1075},"obj":"protein"},{"id":"T15","span":{"begin":1094,"end":1098},"obj":"protein"},{"id":"T16","span":{"begin":1103,"end":1108},"obj":"protein"},{"id":"T17","span":{"begin":1180,"end":1183},"obj":"protein"},{"id":"T18","span":{"begin":1253,"end":1256},"obj":"protein"},{"id":"T19","span":{"begin":1298,"end":1303},"obj":"protein"},{"id":"T20","span":{"begin":1326,"end":1329},"obj":"protein"},{"id":"T21","span":{"begin":1330,"end":1334},"obj":"protein"},{"id":"T22","span":{"begin":1354,"end":1357},"obj":"protein"}],"text":"The X-ray structure of a growth hormone-prolactin receptor complex.\nThe human pituitary hormones, growth hormone (hGH) and prolactin (hPRL), regulate a large variety of physiological processes, among which are growth and differentiation of muscle, bone and cartilage cells, and lactation. These activities are initiated by hormone-receptor binding. The hGH and hPRL receptors (hGHR and hPRLR, respectively) are single-pass transmembrane receptors from class 1 of the haematopoietic receptor superfamily. This classification is based on sequence similarity in their extracellular domains, notably a highly conserved pentapeptide, the so-called 'WSXWS box', the function of which is controversial. All ligands in class 1 activate their respective receptors by clustering mechanisms. In the case of hGH, activation involves receptor homodimerization in a sequential process: the active ternary complex containing one ligand and two receptor molecules is formed by association of a receptor molecule to an intermediate 1:1 complex. hPRL does not bind to the hGH receptor, but hGH binds to both the hGHR and hPRLR, and mutagenesis studies have shown that the receptor-binding sites on hGH overlap. We present here the crystal structure of the 1:1 complex of hGH bound to the extracellular domain of the hPRLR. Comparisons with the hGH-hGHR complex reveal how hGH can bind to the two distinctly different receptor binding surfaces."}