title: Presenilin adopts the ClC channel fold.
abstract: 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 calcium leak channel.
authors.affiliation: Department of Biochemistry, Brandeis University, Waltham, Massachusetts, 02453.
authors.forename: Douglas L
authors.initials: DL
authors.lastname: Theobald
mesh_terms: D000818:Animals; D018118:Chloride Channels / Q000737:chemistry*; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D053763:Presenilins / Q000737:chemistry*; D017510:Protein Folding; D017433:Protein Structure, Secondary; D013329:Structure-Activity Relationship
chemical_list: D018118:Chloride Channels; D053763:Presenilins
keywords: ClC channel; calcium leak channel; presenilin; protein fold