Structural Basis for Molecular Recognition at Serotonin Receptors
| Autor: | Chenghai Zhang, Vsevolod Katritch, Karsten Melcher, Vadim Cherezov, Jinming Ma, Daniel Wacker, Fang Bai, Raymond C. Stevens, John D. McCorvy, X. Edward Zhou, Eyal Vardy, Gye Won Han, Hualiang Jiang, H. Eric Xu, Xi Ping Huang, Huixian Wu, Bryan L. Roth, Xiang Gao, Wei Liu, Huaiyu Yang, Yi Jiang, Chong Wang, Linlin Yang |
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| Rok vydání: | 2013 |
| Předmět: |
Models
Molecular Agonist Protein Folding Protein Conformation medicine.drug_class Stereochemistry Molecular Sequence Data Crystallography X-Ray Ligands Serotonergic Molecular Docking Simulation Protein Structure Secondary Article Protein structure Ergotamine medicine Humans Amino Acid Sequence Binding site Receptor 5-HT receptor Binding Sites Multidisciplinary Chemistry Norfenfluramine Hydrogen Bonding Serotonin 5-HT1 Receptor Agonists Propranolol Tryptamines Lysergic Acid Diethylamide Mutagenesis Docking (molecular) Pindolol Receptor Serotonin 5-HT1B Hydrophobic and Hydrophilic Interactions Dihydroergotamine |
| Zdroj: | Science. 340:610-614 |
| ISSN: | 1095-9203 0036-8075 |
| DOI: | 10.1126/science.1232807 |
| Popis: | Dissecting Serotonin Receptors Serotonin receptors are the targets for many widely used drugs prescribed to treat ailments from depression to obesity and migraine headaches (see the Perspective by Palczewski and Kiser ). C. Wang et al. (p. 610 , published online 21 March) and Wacker et al. (p. 615 , published online 21 March) describe crystal structures of two members of the serotonin family of receptors bound to antimigraine medications or to a precursor of the hallucinogenic drug LSD. Subtle differences in the way particular ligands bind to the receptors cause substantial differences in the signals generated by the receptor and the consequent biological responses. The structures reveal how the same ligand can activate one or both of the two main serotonin receptor signaling mechanisms, depending on which particular receptor it binds. |
| Databáze: | OpenAIRE |
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