PerspectiveMolecular Biology

Folding unpredicted

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Science  06 Dec 2019:
Vol. 366, Issue 6470, pp. 1194-1195
DOI: 10.1126/science.aaz8642

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Summary

Cornichon homologs (CNIHs) are a family of highly conserved small membrane proteins (140 to 160 amino acids in length) that serve as shuttle(s) for the export of proteins from the endoplasmic reticulum (ER) and/or as auxiliary subunits that control the building and gating of AMPA-type glutamate receptors (AMPARs) in the brain. According to predictions from databases and algorithms, CNIHs exhibit a three-transmembrane (TM) domain topology with the protein's amino terminus facing the cytoplasm. On page 1259 of this issue, Nakagawa pre-sents the cryo–electron microscopy (cryo-EM) structure of a CNIH protein in complex with a glutamate receptor (1). The results prove database predictions wrong and provide a structural key to the diverse functions of the cornichon family of proteins.

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