Just Accepted
This article has been peer reviewed and accepted for publication. It is in production and has not been edited, so may differ from the final published form.
Investigating the CaV1.1 II-III loop region by NMR
Abstract
Structural advances in the study of large ion channel proteins continues to progress at a rapid pace giving rise to an ever-increasing number of atomic resolution structures in the protein database. However, despite this progress, unstructured loop regions associated with ion channels often remain structurally invisible. Given that these seemingly unstructured loop regions are often determinant factors in how ion channels function, it is important explore a variety of techniques which may shed light upon their structural make-up. NMR is a versatile technique that can be exploited to structurally interrogate intrinsically disordered loop regions such as those found in ion channels. In this review we examine a range of NMR techniques to explore the structural characteristics of an intrinsically disordered loop (II-III loop) in the skeletal voltage gated ion channel (CaV1.1). Not only do we elucidate the structural properties of this disordered loop, but also show how NMR can be used to study the relationship with its protein binding partners thereby providing mechanistic insights into skeletal muscle function as well as aid in the design of novel therapeutics.
CH25140 Accepted 07 October 2025
© CSIRO 2025
