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Titolo:
Parathyroid hormone and parathyroid hormone-related protein: Model systemsfor the development of an osteoporosis therapy
Autore:
Mierke, DF; Pellegrini, M;
Indirizzi:
Brownence,, Dept Mol Pharmacol Physiol & Biotechnol, Div Biol & Med, Provid Brown Univ Providence RI USA 02912 l & Biotechnol, Div Biol & Med, Provid Brown Univ, Dept Chem, Providence, RI 02912 USA Brown Univ Providence RI USA 02912 v, Dept Chem, Providence, RI 02912 USA
Titolo Testata:
CURRENT PHARMACEUTICAL DESIGN
fascicolo: 1, volume: 5, anno: 1999,
pagine: 21 - 36
SICI:
1381-6128(199901)5:1<21:PHAPHP>2.0.ZU;2-W
Fonte:
ISI
Lingua:
ENG
Soggetto:
(PTH)/PTH-RELATED PEPTIDE RECEPTOR; PTH-RELATED PEPTIDE; NUCLEAR-MAGNETIC-RESONANCE; 3RD CYTOPLASMIC LOOP; MOLECULAR-DYNAMICS SIMULATIONS; VASOACTIVE-INTESTINAL-PEPTIDE; INHIBITS BONE-RESORPTION; STABILIZED NMR STRUCTURE; HUMAN PTH/PTHRP RECEPTOR; GLUCAGON-LIKE PEPTIDE-1;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
175
Recensione:
Indirizzi per estratti:
Indirizzo: Mierke, DF Brown Univ, Dept Mol Pharmacol, Div Biol & Med, Providence, RI 02912 USA Brown Univ Providence RI USA 02912 d, Providence, RI 02912 USA
Citazione:
D.F. Mierke e M. Pellegrini, "Parathyroid hormone and parathyroid hormone-related protein: Model systemsfor the development of an osteoporosis therapy", CUR PHARM D, 5(1), 1999, pp. 21-36

Abstract

The parathyroid hormone (PTH) plays a vital role in the homeostasis of calcium within the blood stream. Given its unique ability to increase bone density, an understanding of the molecular mechanism by which the hormone is recognized and binds to its receptor should provide targets for the development of PTH-based, anabolic agents for the treatment of osteoporosis. Parathyroid hormone related protein (PTHrP), a genetically and structurally distinct hormone which displays similar binding and activation profiles as PTH, has greatly facilitated the effort to establish a structure-biological function relationship by allowing for direct comparisons. In an analogous manner, the presence of two receptors, PTH/PTHrP (PTH1) and PTH2. which differ in their ligand selectivity (PTH2 is activated by PTH, not PTHrP) has provided a unique vehicle for probing the structural motifs of the receptor required for ligand recognition and binding. Recent photo-affinity cross-linkingstudies of PTH and PTHrP binding to PTH1 have produced direct points of contact between the ligand and receptor. Here, we review each of the components involved in this important hormone system, with particular emphasis on the structural features of each: the ligands (PTH and PTHrP)I the receptors (PTH1 and PTH2), and the interaction between ligand and receptor. Although the current understanding of the molecular mechanism of ligand binding and receptor activation does not allow for the rational design of drug candidates, and indeed contains much conjecture, significant strides have been madetowards this end.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 13/07/20 alle ore 06:43:39