Insights into the molecular recognition of the granuphilin C2A domain with PI(4,5)P2
Copyright policy )Insights into the molecular recognition of the granuphilin C2A domain with PI(4,5)P2
Phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) is a key player in regulating the process of excytosis, including insulin secretion. Granuphilin, a tandem C2 domain containing protein, mediates the docking of insulin granules onto plasma membrane. The C2A domain plays key roles in this process through interaction with PI(4,5)P2. In this study, we have investigated the molecular recognition mechanism of granuphilin-C2A domain to PI(4,5)P2 head group, and further to PI(4,5)P2-nanodisc by NMR, ITC, MST and SEC methods. Our results demonstrate that PI(4,5)P2 binds to the concave surface of granuphilin-C2A domain. The key residues involved in the binding were validated by mutation analysis.
- Chinese Academy of Sciences China (People's Republic of)
- Dalian Institute of Chemical Physics China (People's Republic of)
- Hefei Institutes of Physical Science China (People's Republic of)
- University of Science and Technology of China China (People's Republic of)
- State Key Laboratory of Molecular Reaction Dynamics China (People's Republic of)
Molecular Docking Simulation, Phosphatidylinositol Phosphates, Molecular Sequence Data, Vesicular Transport Proteins, Humans, Amino Acid Sequence, Nuclear Magnetic Resonance, Biomolecular, Protein Structure, Tertiary
Molecular Docking Simulation, Phosphatidylinositol Phosphates, Molecular Sequence Data, Vesicular Transport Proteins, Humans, Amino Acid Sequence, Nuclear Magnetic Resonance, Biomolecular, Protein Structure, Tertiary
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