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Schlagwörter:
B2-Rezeptor; Ligandenbindung; Membranproteine; NMR-Spektroskopie; Proteinstrukturen
Zusammenfassung:
G‐protein coupled receptors (GPCRs) are responsible for a large number of physiological processes, such as sensory transduction, mediation of hormonal activity, and cell‐to‐cell communication.1, 2 GPCRs are membrane proteins with seven transmembrane helices and are the target of some 50 % of modern drugs. They constitute the largest known protein family and have had more than 800 species identified in the search for medical solutions to human illnesses.3, 4 However, owing to the lack of three‐dimensional structures, structure‐based drug design has not been possible. To date, the structures of only two GPCRs have been solved.5, 6 Pharmacological research aimed at GPCRs is therefore restricted to mostly computational and experimental trial‐and‐error approaches.7 This limitation could be potentially overcome by determining the structures of bound agonists, which activate GPCRs, and using these as structural templates for drug design. To do so, the availability of GPCRs needs to be increased.7–9 Herein, we describe the backbone structure of the agonist bradykinin bound to the human bradykinin B2 receptor, which was determined by solid‐state NMR spectroscopy. This is only the second detailed investigation of its kind.
