Structural models of the NaPi-II sodium-phosphate cotransporters.

ABSTRACT: Progress towards understanding the molecular mechanisms of phosphate homeostasis through sodium-dependent transmembrane uptake has long been stymied by the absence of structural information about the NaPi-II sodium-phosphate transporters. For many other coupled transporters, even those unrelated to NaPi-II, internal repeated elements have been revealed as a key feature that is inherent to their function. Here, we review recent structure prediction studies for NaPi-II transporters. Attempts to identify structural templates for NaPi-II transporters have leveraged the structural repeat perspective to uncover an otherwise obscured relationship with the dicarboxylate-sodium symporters (DASS). This revelation allowed the prediction of three-dimensional structural models of human NaPi-IIa and flo

SUBMITTER: Fenollar-Ferrer C 

PROVIDER: S-EPMC6325988 | biostudies-literature | 2019 Jan

REPOSITORIES: biostudies-literature