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- W2999693663 abstract "Stimulation of C-type lectin domain of human dectin-1 receptor by fungal β-glucans causes conformational changes in its cytoplasmic domain which initiates various cellular responses mediated by downstream signaling components. We aimed to build the three-dimensional structures of the cytoplasmic domain as well as C-type lectin domain of human Dectin-1along with their potential ligands through homology modeling.The overall three-dimensional fold of cytoplasmic domain was found to consist of mixed β-sheet whereas,in case of C-type lectin domain antiparallel β-sheets flanked by α-helices were observed. Protein-protein docking strategy was utilized to monitorkey interactions between cytoplasmic domainof dectin-1 receptor and PKCδ, as a prime regulator of Dectin-1 signaling. The interface was observed to have both hydrophilic and hydrophobic amino acid residues maintaining crucial contacts between the two proteins. The given three dimensional structural information can be implicated in structure-based drug designing to discover potential immunomodulators that can interfere with the immune responses and phagocytosis during inflammatory and infectious conditions." @default.
- W2999693663 created "2020-01-23" @default.
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- W2999693663 date "2019-07-01" @default.
- W2999693663 modified "2023-09-23" @default.
- W2999693663 title "Structural investigation of human dectin-1 receptor; A novel gateway in drug discovery." @default.
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