The Structural Basis of Arrestin Functions
Language: English
Published by Springer, 2017
- Hardcover
- New
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- Title
- The Structural Basis of Arrestin Functions
- Publisher
- Springer
- Publication year
- 2017
- Condition
- New
- Binding
- Hardcover
- Language
- English
- ISBN 10
- 331957552X
- ISBN 13
- 9783319575520
This volume summarizes our current understanding of the structural basis of the functions of arrestin family of proteins. Arrestins were first discovered as key players in the desensitization of G protein-coupled receptors (GPCRs). Recent studies showed that arrestins are important signal transducers in their own right, organizing multi-protein complexes and scaffolding numerous signaling cascades that regulate cell proliferation, differentiation, and apoptotic death.
Here arrestin functions are described primarily from the structural prospective. The book covers basal structure of arrestin proteins, receptor binding-induced conformational changes in arrestins, as well as the structure of “pre-activated” mutants. Particular focus is on the arrestin elements interacting with numerous binding partners, GPCRs and cytoplasmic signaling proteins. We expect that this information and insights will help to understand and exploit the phenomenon of signaling bias, which is a new promising direction in drug discovery.
The chapters are written by the world-class specialists in the field, mostly the people who actually contributed the data discussed. The book gives coherent historical prospective and describes the most recent findings.
The book would be particularly useful for scientists in academia and industry working in the fields of pharmacology, cell biology, structural biology, and drug discovery. We expect that the focus on the molecular basis of protein-protein interactions would help to develop novel tools for engaging this important type of targets for research and therapeutic purposes.
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About the Author
Dr. Gurevich got his PhD in Bioorganic Chemistry at the Shemyakin Institute in Moscow. He studied structure and function of arrestin proteins since he joined the lab of Dr. Benovic as a post-doc in 1991. Dr. Gurevich’s studies revealed why arrestins prefer active phosphorylated GPCRs and how they sense receptor-attached phosphates. His lab constructed phosphorylation-independent arrestin mutants and tested their ability to compensate for the defects of GPCR phosphorylation. His lab elucidated the structural basis of arrestin preference for particular GPCRs and constructed the first non-visual arrestins with high receptor specificity. In collaboration with different crystallographers Dr. Gurevich’s lab solved the structures of all four vertebrate arrestins in basal conformation and the structure of the arrestin-rhodopsin complex.
"About the title" may belong to another edition of this title.
Books Puddle
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