Neutrophils play major phagocytes that participate in the various effector phase of immunity. Mannsoe binding lectin (MBL) assisted priming of neutrophils could trigger various processes including modulation of endocytosis rate, reactive oxygen production chemotaxix etc, through interactions with cell surface receptors. The physiological receptor for MBL on neutrophils surface are still unreported. As macromolecular docking could be attempted to determine the protein-protein interactions which are important for understanding cellular function and organization. Study was performed to identify the interacting partner of MBL present on neutrophils surface which leads to the activation of various cell processes. Protein network analysis, homology modeling and Rigid docking were performed to explore structural features and binding mechanism of MBL with its cellular receptors. The results indicates that CR1 interact with the MBL and leads to activation of the neutrophils.
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