G Protein-Coupled Receptors
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G protein-coupled receptors (GPCRs) constitute the largest family of cell-surface receptors, with more than 800 members identified thus far in the human genome. They regulate the function of most cells in the body, and represent approximately 3% of the genes in the human genome. These receptors respond to a wide variety of structurally diverse ligands, ranging from small molecules, such as biogenic amines, nucleotides and ions, to lipids, peptides, proteins and even light. Ligands (agonists and antagonists) acting on GPCRs are important commonly used in drug therapy of numerous diseases,…mehr

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Produktbeschreibung
G protein-coupled receptors (GPCRs) constitute the largest family of cell-surface receptors, with more than 800 members identified thus far in the human genome. They regulate the function of most cells in the body, and represent approximately 3% of the genes in the human genome. These receptors respond to a wide variety of structurally diverse ligands, ranging from small molecules, such as biogenic amines, nucleotides and ions, to lipids, peptides, proteins and even light. Ligands (agonists and antagonists) acting on GPCRs are important commonly used in drug therapy of numerous diseases, including cardiovascular and mental disorders, retinal degeneration, cancer, and AIDS. It is estimated that these receptors represent about one third of the actual identified targets of clinically used drugs. This book, which lies between the fields of chemical biology, molecular pharmacology and medicinal chemistry, is divided into three parts. The first part considers what receptor structures tell us about the mechanism of receptor activation. Part II focuses on receptor function. It discusses what the data from biophysical and mutational studies, and the analysis of the interactions of the receptor with ligands and regulator proteins, tell us about the process of signal transduction. The final part, on modelling and simulation, details what new insights on the link between structure and mechanism can be provided by theoretical studies and their implications in drug design. The various chapters present an update on the latest developments in GPCR structures and detailed structural changes linked to activation. They cover the latest news of the extraordinary complex function of these receptors, concentrating on the many aspects that are currently revolutionizing our current views of these proteins: receptor constitutive activity, receptor oligomerization, functional selectivity, biased agonism, multiple signalling pathways, multiple accessory proteins, functional cross talk and the mechanism of signal integration. This complex picture is tackled from complementary experimental and theoretical approaches, which represent a clear statement of our current knowledge of the GPCR complexity.
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Autorenporträt
Jes·s Giraldo is based at the Institut de NeurociÞncies and Unitat de BioestadÝstica, Universitat Aut=noma de Barcelona. He works mainly in the field of mathematical modelling of GPCRs and has collaborated with a number of experimentalists, some of them leaders in the GPCR field. This has given him a deep understanding of the relationships between theory and experimentation in the area and a holistic view of the topic. Jean-Philippe Pin got his PhD in Molecular Biology from the University of Montpellier 2, France. He participated in the discovery of the metabotropic glutamate receptors and demonstrated synergism between various glutamate receptor subtypes for the activation of phospholipase A2. Subsequently, he worked as a post doctoral fellow at the Salk Institute where he cloned and characterized new mGlu receptor splice variants. In 1992, he set up a research team working on the structure function relationship of mGlu receptors in the CNRS laboratory in Montpellier. Currently, he heads the Molecular Pharmacology Department within the Institute of Functional Genomics, Montpellier, France where his research focuses on the molecular and cellular dynamics of GPCRs and has led to major new concepts in the GPCR field.