Ligand-free SpSLC9C1 in detergent
Ontology highlight
ABSTRACT:
SUBMITTER: Cristina Paulino
PROVIDER: EMPIAR-11629 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
Structures of a sperm-specific solute carrier gated by voltage and cAMP.
Kalienkova Valeria V Peter Martin F MF Rheinberger Jan J Paulino Cristina C
Nature 20231025 7985
The newly characterized sperm-specific Na<sup>+</sup>/H<sup>+</sup> exchanger stands out by its unique tripartite domain composition<sup>1,2</sup>. It unites a classical solute carrier unit with regulatory domains usually found in ion channels, namely, a voltage-sensing domain and a cyclic-nucleotide binding domain<sup>1,3</sup>, which makes it a mechanistic chimera and a secondary-active transporter activated strictly by membrane voltage. Our structures of the sea urchin SpSLC9C1 in the absence ...[more]
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