Advances in Diabetes and Metabolism(CEASE PUBLICATION) Vol. 4(2), pp. 32 - 43
DOI: 10.13189/adm.2016.040202
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In Silico Structure Analysis of Type 2 Diabetes Associated Cysteine Protease Calpain-10 (CAPN10)

Rajneesh Prajapat ^*, Ijen Bhattacharya
Department of Medical Biochemistry, Faculty of Medical Sciences, Rama Medical College, Rama University, India

ABSTRACT

Calpain-10 (CAPN10) is a cysteine protease that is known to hydrolyze specific substrates significant for calcium-regulated signaling pathways and it's activated by intracellular calcium (Ca²⁺). The calpain10 is known to be involved in the cellular degenerative processes that characterize several diseases such as cancer, stroke and heart attack. The role of calpain10 was recently identified and associated with diabetes mellitus type 2. In this paper, the homology modelling procedure was used to determine the 3D structure of human calpain10 (AAH07553). The μ-calpain (1QXP) of Rattus norvegicus was selected as a template for the construction of calpain10 model. Ramachandran plot of calpain10 (AAH07553) has only 55.9% residues in the most favored regions, while template μ-calpain (1QXP) has 69.3% residues in the most favored regions. The model was validated by using protein structure tools RAMPAGE and Prochek for reliability. 3D structure of calpain10 suggested its active site remains conserved among family members and the major interactions are similar to those observed for the template (1QXP).

KEYWORDS
Calpain 10, Type II Diabetes, Homology Modelling

Cite This Paper in IEEE or APA Citation Styles
(a). IEEE Format:
[1] Rajneesh Prajapat , Ijen Bhattacharya , "In Silico Structure Analysis of Type 2 Diabetes Associated Cysteine Protease Calpain-10 (CAPN10)," Advances in Diabetes and Metabolism(CEASE PUBLICATION), Vol. 4, No. 2, pp. 32 - 43, 2016. DOI: 10.13189/adm.2016.040202.

(b). APA Format:
Rajneesh Prajapat , Ijen Bhattacharya (2016). In Silico Structure Analysis of Type 2 Diabetes Associated Cysteine Protease Calpain-10 (CAPN10). Advances in Diabetes and Metabolism(CEASE PUBLICATION), 4(2), 32 - 43. DOI: 10.13189/adm.2016.040202.