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• W2538045770 endingPage "e0164970" @default.
• W2538045770 startingPage "e0164970" @default.
• W2538045770 abstract "Cystatin superfamily is a large group of evolutionarily related proteins involved in numerous physiological activities through their inhibitory activity towards cysteine proteases. Despite sharing the same cystatin fold, and inhibiting cysteine proteases through the same tripartite edge involving highly conserved N-terminal region, L1 and L2 loop; cystatins differ widely in their inhibitory affinity towards C1 family of cysteine proteases and molecular details of these interactions are still elusive. In this study, inhibitory interactions of human family 1 & 2 cystatins with cathepsin L1 are predicted and their stability and viability are verified through protein docking & comparative molecular dynamics. An overall stabilization effect is observed in all cystatins on complex formation. Complexes are mostly dominated by van der Waals interaction but the relative participation of the conserved regions varied extensively. While van der Waals contacts prevail in L1 and L2 loop, N-terminal segment chiefly acts as electrostatic interaction site. In fact the comparative dynamics study points towards the instrumental role of L1 loop in directing the total interaction profile of the complex either towards electrostatic or van der Waals contacts. The key amino acid residues surfaced via interaction energy, hydrogen bonding and solvent accessible surface area analysis for each cystatin-cathepsin L1 complex influence the mode of binding and thus control the diverse inhibitory affinity of cystatins towards cysteine proteases." @default.
• W2538045770 created "2016-10-28" @default.
• W2538045770 creator A5025762583 @default.
• W2538045770 creator A5072260411 @default.
• W2538045770 date "2016-10-20" @default.
• W2538045770 modified "2023-09-25" @default.
• W2538045770 title "Structural Dynamics Investigation of Human Family 1 & 2 Cystatin-Cathepsin L1 Interaction: A Comparison of Binding Modes" @default.
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• W2538045770 doi "https://doi.org/10.1371/journal.pone.0164970" @default.
• W2538045770 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5072729" @default.
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• W2538045770 hasPublicationYear "2016" @default.
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