Cryo-EM structures of the human volume-regulated anion channel LRRC8 View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2018-09

AUTHORS

Go Kasuya, Takanori Nakane, Takeshi Yokoyama, Yanyan Jia, Masato Inoue, Kengo Watanabe, Ryoki Nakamura, Tomohiro Nishizawa, Tsukasa Kusakizako, Akihisa Tsutsumi, Haruaki Yanagisawa, Naoshi Dohmae, Motoyuki Hattori, Hidenori Ichijo, Zhiqiang Yan, Masahide Kikkawa, Mikako Shirouzu, Ryuichiro Ishitani, Osamu Nureki

ABSTRACT

Maintenance of cell volume against osmotic change is crucial for proper cell functions. Leucine-rich repeat-containing 8 proteins are anion-selective channels that extrude anions to decrease the cell volume on cellular swelling. Here, we present the structure of human leucine-rich repeat-containing 8A, determined by single-particle cryo-electron microscopy. The structure shows a hexameric assembly, and the transmembrane region features a topology similar to gap junction channels. The LRR region, with 15 leucine-rich repeats, forms a long, twisted arc. The channel pore is located along the central axis and constricted on the extracellular side, where highly conserved polar and charged residues at the tip of the extracellular helix contribute to permeability to anions and other osmolytes. Two structural populations were identified, corresponding to compact and relaxed conformations. Comparing the two conformations suggests that the LRR region is flexible and mobile, with rigid-body motions, which might be implicated in structural transitions on pore opening. More... »

PAGES

797-804

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/s41594-018-0109-6

DOI

http://dx.doi.org/10.1038/s41594-018-0109-6

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1106199540

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/30127360


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