A limited memory algorithm for bound constrained optimization
SIAM Journal on Scientific Computing
ANOLEA: A WWW Server to Assess Protein Structures
Proceedings of the 5th International Conference on Intelligent Systems for Molecular Biology
Introduction to Bioinformatics
Introduction to Bioinformatics
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Calpain-10 (CAPN10) is a cysteine protease that is activated by intracellular calcium (Ca^2^+) and known to be involved in diseases such as cancer, heart attack, and stroke. A role for the CAPN10 gene in diabetes mellitus type II was recently identified. Hyper activation of the enzyme initiates a series of destructive cycles that can cause irreversible damage to cells. The development of inhibitors may be useful as therapeutic agents for a number of calpainopathies. In this paper, we have used the homology modelling technique to determine the 3D structure of calpain-10 from Homo sapiens. The model of calpain-10 obtained by homology modelling suggests that its active site is conserved among family members and the main interactions are similar to those observed for @m-calpain. Structural analysis revealed that there are small differences in the charge distribution and molecular surface of the enzyme. These differences are probably less dependent on calcium for calpain-10 than they are for @m-calpain. In addition, the ion pair Cys^-/His^+ formation was observed using of Molecular Dynamics (MD) simulations that were based upon hybrid quantum mechanical/molecular mechanical (QM/MM) approaches. Finally, the binding of the SNJ-1715 inhibitor to calpain-10 was investigated in order to further understand the mechanism of inhibition of calpain-10 by this inhibitor at the molecular level.