A theoretical investigation into the lipid interactions of m-calpain.
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.
Daman
A
A
Department of Physics, Maths and Astronomy, University of Central Lancashire, Preston, UK.
Harris
F
F
Biswas
S
S
Wallace
J
J
Phoenix
D A
DA
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
D002154:Calpain