Cryo-EM structure of phosphodiesterase 6 reveals insights into the allosteric regulation of type I phosphodiesterases
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ABSTRACT:
SUBMITTER: Sahil Gulati
PROVIDER: EMPIAR-10228 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
Cryo-EM structure of phosphodiesterase 6 reveals insights into the allosteric regulation of type I phosphodiesterases.
Gulati Sahil S Palczewski Krzysztof K Engel Andreas A Stahlberg Henning H Kovacik Lubomir L
Science advances 20190227 2
Cyclic nucleotide phosphodiesterases (PDEs) work in conjunction with adenylate/guanylate cyclases to regulate the key second messengers of G protein-coupled receptor signaling. Previous attempts to determine the full-length structure of PDE family members at high-resolution have been hindered by structural flexibility, especially in their linker regions and N- and C-terminal ends. Therefore, most structure-activity relationship studies have so far focused on truncated and conserved catalytic dom ...[more]
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