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Publication Abstract from PubMed

Piezo has recently been identified as a family of eukaryotic mechanosensitive channels composed of subunits containing over 2,000 amino acids, without recognizable sequence similarity to other channels. Here, we present the crystal structure of a large, conserved extramembrane domain located just before the last predicted transmembrane helix of C. elegans PIEZO, which adopts a topologically distinct beta sandwich fold. The structure was also determined of a point mutation located on a conserved surface at the position equivalent to the human PIEZO1 mutation found in dehydrated hereditary stomatocytosis patients (M2225R). While the point mutation does not change the overall domain structure, it does alter the surface electrostatic potential that may perturb interactions with a yet-to-be-identified ligand or protein. The lack of structural similarity between this domain and any previously characterized fold, including those of eukaryotic and bacterial channels, highlights the distinctive nature of the Piezo family of eukaryotic mechanosensitive channels.

The Structure of a Conserved Piezo Channel Domain Reveals a Topologically Distinct beta Sandwich Fold.,Kamajaya A, Kaiser JT, Lee J, Reid M, Rees DC Structure. 2014 Sep 17. pii: S0969-2126(14)00254-8. doi:, 10.1016/j.str.2014.08.009. PMID:25242456^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.