Please use this identifier to cite or link to this item: http://localhost:80/xmlui/handle/123456789/16000
Title: Structural investigation of human dectin-1 receptor; A novel gateway in drug discovery
Authors: Talat Roome
Yasmeen Rashid
Muhammad Aurongzeb
Anam Razzak
Keywords: C-type lectin domain
cytoplasmic domain of Dectin-1 receptor
structural bioinformatics
homology modeling
molecular docking
Issue Date: 8-Jul-2019
Publisher: Karachi: Faculty of Pharmacy & Pharmaceutical Sciences University of Karachi
Citation: Roome, T., Rashid, Y., Aurongzeb, M., & Razzak, A. (2019). Structural investigation of human dectin-1 receptor; A novel gateway in drug discovery. Pakistan Journal of Pharmaceutical Sciences, 32(4).
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 thecytoplasmic domain as well asC-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 βsheets flanked byα-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.
URI: http://142.54.178.187:9060/xmlui/handle/123456789/16000
ISSN: 1011-601X
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