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            <title xml:lang="en">Structure and dynamics of dynorphin peptide and its receptor</title>
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            <idno type="halRefHtml">Gerald Litwack. &lt;i&gt;Opioid Hormones&lt;/i&gt;, 111, &lt;a target="_blank" href="https://www.sciencedirect.com/science/article/abs/pii/S0083672919300421?via%3Dihub"&gt;Elsevier&lt;/a&gt;, pp.17-47, In press, &lt;a target="_blank" href="https://dx.doi.org/10.1016/bs.vh.2019.05.006"&gt;&amp;#x27E8;10.1016/bs.vh.2019.05.006&amp;#x27E9;&lt;/a&gt;</idno>
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            <idno type="stamp" n="IPBS">Institut de Pharmacologie et de Biologie Structurale</idno>
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                <term xml:lang="en">X-ray crystallography</term>
                <term xml:lang="en">drug design</term>
                <term xml:lang="en">docking</term>
                <term xml:lang="en">molecular dynamics</term>
                <term xml:lang="en">electron microscopy</term>
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                <term xml:lang="en">heterologous expression systems</term>
                <term xml:lang="en">site-directed mutagenesis</term>
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                <term xml:lang="en">membrane protein</term>
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              <p>Dynorphin is a neuropeptide involved in pain, addiction and mood regulation. It exerts its activity by binding to the kappa opioid receptor (KOP) which belongs to the large family of G-protein coupled receptors. The dynorphin peptide was discovered in 1975, while its receptor was cloned in 1993. This review will describe: a) the activities and physiological functions of dynorphin and its receptor, b) early structure-activity relationship studies performed before cloning of the receptor (mostly pharmacological and biophysical studies of peptide analogues), c) structure-activity relationship studies performed after cloning of the receptor via receptor mutagenesis and the development of recombinant receptor expression systems, d) structural biology of the opiate receptors culminating in X-ray structures of the four opioid receptors in their inactive state and structures of MOP and KOP receptors in their active state. X-ray and EM structures are combined with NMR data, which gives complementary insight into receptor and peptide dynamics. Molecular modelling greatly benefited from the availability of atomic resolution 3D structures of receptor-ligand complexes and an example of the strategy used to model a dynorphin-KOP receptor complex using NMR data will be described. These achievements have led to a better understanding of the complex dynamics of KOP receptor activation and to the development of new ligands and drugs.</p>
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