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Literature DB >> 11681718

A theoretical investigation into the lipid interactions of m-calpain.

A Daman¹, F Harris, S Biswas, J Wallace, D A Phoenix.

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.

Entities: Chemical Gene

Mesh：

Substances：
Calpain

Year: 2001 PMID： 11681718 DOI： 10.1023/a:1017939116715

Source DB: PubMed Journal: Mol Cell Biochem ISSN： 0300-8177 Impact factor: 3.396

30 in total

1. Crystal structure of calpain reveals the structural basis for Ca(2+)-dependent protease activity and a novel mode of enzyme activation.

Authors: C M Hosfield; J S Elce; P L Davies; Z Jia
Journal: EMBO J Date: 1999-12-15 Impact factor: 11.598

2. Use of helical wheels to represent the structures of proteins and to identify segments with helical potential.

Authors: M Schiffer; A B Edmundson
Journal: Biophys J Date: 1967-03 Impact factor: 4.033

Review 3. Calpains: intact and active?

Authors: G V Johnson; R P Guttmann
Journal: Bioessays Date: 1997-11 Impact factor: 4.345

4. Activation of calpain in lens: a review and proposed mechanism.

Authors: M Azuma; C Fukiage; L L David; T R Shearer
Journal: Exp Eye Res Date: 1997-04 Impact factor: 3.467

5. An algorithm for the detection of surface-active alpha helices with the potential to anchor proteins at the membrane interface.

Authors: M G Roberts; D A Phoenix; A R Pewsey
Journal: Comput Appl Biosci Date: 1997-02

Review 6. Regulation of the calpain-calpastatin system by membranes (review).

Authors: H Kawasaki; S Kawashima
Journal: Mol Membr Biol Date: 1996 Oct-Dec Impact factor: 2.857

Review 7. Structure and physiological functions of ubiquitous and tissue-specific calpain species. Muscle-specific calpain, p94, interacts with connectin/titin.

Authors: H Sorimachi; S Kimura; K Kinbara; J Kazama; M Takahashi; H Yajima; S Ishiura; N Sasagawa; I Nonaka; H Sugita; K Maruyama; K Suzuki
Journal: Adv Biophys Date: 1996

8. Positive regulation of mu-calpain action by polyphosphoinositides.

Authors: T C Saido; M Shibata; T Takenawa; H Murofushi; K Suzuki
Journal: J Biol Chem Date: 1992-12-05 Impact factor: 5.157

9. Mutational analysis of the fusion peptide of the human immunodeficiency virus type 1: identification of critical glycine residues.

Authors: M D Delahunty; I Rhee; E O Freed; J S Bonifacino
Journal: Virology Date: 1996-04-01 Impact factor: 3.616