| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 8330624 | International Journal of Biological Macromolecules | 2015 | 4 Pages |
Abstract
Mannose binding lectin (MBL) is a collectin with C-terminus Carbohydrate Recognition Domain (CRD) which binds with pathogen and arbitrate functions like activation of complement pathway, opsonization etc. The CRD required Ca2+ ions to recognize the sugar moieties. In the present study the binding properties of CRD with divalent ions were characterized by Electron Paramagnetic Resonance (EPR) spectroscopy. The results revealed that the metal binding site of CRD is of approximately 1Â Ã
diameter and ions greater than the size are not able to enter.
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Authors
Pankaj Kumar Patel, Maliram Hindala, Bavita Kohli, Krishnan Hajela,