Ontology highlight
ABSTRACT:
SUBMITTER: Theobald DL
PROVIDER: S-EPMC4918416 | biostudies-literature | 2016 Jul
REPOSITORIES: biostudies-literature
Protein science : a publication of the Protein Society 20160323 7
Presenilin is an integral membrane aspartate protease that regulates cellular processes by cleaving proteins within the cell membrane. The recent crystal structure of presenilin reveals a conspicuous pore in a bundle of nine α-helices, which was originally thought to adopt a novel protein fold. However, here I show that the presenilin fold is a variant of the ClC chloride channel/transporter fold. This observation may have important implications for presenilin's postulated biological role as a c ...[more]