Isothermal Titration Calorimetry for Fragment-Based Analysis of Ion Channel Interactions
- PMID: 38856907
- DOI: 10.1007/978-1-0716-3818-7_16
Isothermal Titration Calorimetry for Fragment-Based Analysis of Ion Channel Interactions
Abstract
Ion channels are membrane proteins that may also have intracellular and extracellular domains that interact with other ligands. In many cases, these interaction sites are highly mobile and may undergo changes in the configuration upon binding with regulatory signaling molecules. Isothermal titration calorimetry (ITC) is a powerful technique to quantify protein-ligand interactions of purified samples in solution. This chapter describes a fragment-based analysis method using ITC to quantify the interactions between a domain of the voltage-gated Kv7 channel and the calcium-regulated protein calmodulin. This example can be used to quantify the interactions between specific domains of other ion channels and their regulatory signaling proteins.
Keywords: Calmodulin; Fragment-based analysis; G-protein; Isothermal titration calorimetry; Kv7; Peptides.
© 2024. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.
References
-
- Falkenburger BH, Jensen JB, Dickson EJ, Suh BC, Hille B (2010) Phosphoinositides: lipid regulators of membrane proteins. J Physiol 588(Pt 17):3179–3185. https://doi.org/10.1113/jphysiol.2010.192153 - DOI - PubMed - PMC
-
- Hammond GRV, Burke JE (2020) Novel roles of phosphoinositides in signaling, lipid transport, and disease. Curr Opin Cell Biol 63:57–67. https://doi.org/10.1016/j.ceb.2019.12.007 - DOI - PubMed - PMC
-
- Hilgemann DW, Feng S, Nasuhoglu C (2001) The complex and intriguing lives of PIP2 with ion channels and transporters. Sci STKE 2001(111):re19. https://doi.org/10.1126/stke.2001.111.re19 - DOI - PubMed
-
- Saimi Y, Kung C (2002) Calmodulin as an ion channel subunit. Annu Rev Physiol 64:289–311. https://doi.org/10.1146/annurev.physiol.64.100301.111649 - DOI - PubMed
-
- Sheng M, Kim E (1996) Ion channel associated proteins. Curr Opin Neurobiol 6(5):602–608. https://doi.org/10.1016/s0959-4388(96)80091-2 - DOI - PubMed
MeSH terms
Substances
Grants and funding
LinkOut - more resources
Full Text Sources
