Critical amino acid residues regulating TRPA1 Zn²⁺ response: A comparative study across species.

ABSTRACT: Cellular zinc ions (Zn²⁺) are crucial for signal transduction in various cell types. The transient receptor potential (TRP) ankyrin 1 (TRPA1) channel, known for its sensitivity to intracellular Zn²⁺ ([Zn²⁺]_i), has been a subject of limited understanding regarding its molecular mechanism. Here, we used metal ion-affinity prediction, three-dimensional structural modeling, and mutagenesis, utilizing data from the Protein Data Bank and AlphaFold database, to elucidate the [Zn²⁺]_i binding domain (IZD) structure composed by specific AAs residues in human (hTRPA1) and chicken TRPA1 (gTRPA1). External Zn²⁺ induced activation in hTRPA1, while not in gTRPA1. Moreover, external Zn²⁺ elevated [Zn²⁺]

SUBMITTER: Matsubara M 

PROVIDER: S-EPMC11134551 | biostudies-literature | 2024 Jun

REPOSITORIES: biostudies-literature