title: A theoretical investigation into the lipid interactions of m-calpain.
abstract: The protease, m-calpain, has been implicated in a number of pathological conditions. The enzyme is a calcium-dependent heterodimer whose activity appears to be modulated by membrane interaction involving a segment, TAMRIL, located in domain V of the protein's small subunit. Based on a sequence analysis of m-calpain, using DWIH and hydrophobic moment plot based methodologies, we have shown that this segment may contribute to a lipid interactive, oblique orientated, alpha-helical region. Our results could form a basis for future studies on the postulated lipid modulation of m-calpain activity.
authors.affiliation: Department of Physics, Maths and Astronomy, University of Central Lancashire, Preston, UK.
authors.forename: A
authors.initials: A
authors.lastname: Daman
authors.forename: F
authors.initials: F
authors.lastname: Harris
authors.forename: S
authors.initials: S
authors.lastname: Biswas
authors.forename: J
authors.initials: J
authors.lastname: Wallace
authors.forename: D A
authors.initials: DA
authors.lastname: Phoenix
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002154:Calpain / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D050356:Lipid Metabolism; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary
chemical_list: D002154:Calpain