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Literature summary for 3.4.22.B30 extracted from

  • da Silva, R.C.; de Alencar, N.A.; Alves, C.N.; Lameira, J.
    Analysis of the structure of calpain-10 and its interaction with the protease inhibitor SNJ-1715 (2013), Comput. Biol. Med., 43, 1334-1340.
    View publication on PubMed
Search for more literature for 3.4.22.B30

Application

Application Comment Organism
drug development the development of inhibitors against calpain-10 may be useful as therapeutic agents for a number of calpainopathies Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
N-[(2R)-4-hydroxy-1-oxobutan-2-yl]-N2-(phenylcarbamothioyl)-L-leucinamide binding structure, the inhibitor shows interactions with the Cys115, Gly207, Gly20,8 and Gly271 residues, overview. Reversible intramolecular conversion of the cyclic hemiacetal form of SNJ-1715 to the free aldehyde form Homo sapiens
N-[(3R)-2-hydroxytetrahydrofuran-3-yl]-N2-(phenylcarbamothioyl)-L-leucinamide binding structure, the inhibitor shows interactions with the Cys115, Gly207, Gly20,8 and Gly271 residues, overview. Reversible intramolecular conversion of the cyclic hemiacetal form of SNJ-1715 to the free aldehyde form Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ depedent on, activates Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens Q9HC96 gene CAPN10
-

Synonyms

Synonyms Comment Organism
calpain-10
-
 Homo sapiens
CAPN10
-
 Homo sapiens

General Information

General Information Comment Organism
malfunction hyperactivation of the enzyme initiates a series of destructive cycles that can cause irreversible damage to cells Homo sapiens
metabolism the enzyme is involved in diseases such as cancer, heart attack, and stroke, a role for the CAPN10 gene indiabetes mellitus type II Homo sapiens
additional information three-dimensional enzyme homology modelling, structure comparisons, QM/MM molecular dynamics simulations, overview Homo sapiens