title: Divalent metal ions binding properties of goat serum mannose binding lectin.
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 Ca(2+) 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 1 Å diameter and ions greater than the size are not able to enter.
authors.affiliation: School of Life Sciences, Devi Ahilya University, Indore, India.
authors.forename: Pankaj Kumar
authors.initials: PK
authors.lastname: Patel
authors.affiliation: School of Life Sciences, Devi Ahilya University, Indore, India.
authors.forename: Maliram
authors.initials: M
authors.lastname: Hindala
authors.affiliation: School of Life Sciences, Devi Ahilya University, Indore, India; Department of Bio-Technology, ISLE, IPS Academy, Indore, India.
authors.forename: Bavita
authors.initials: B
authors.lastname: Kohli
authors.affiliation: School of Life Sciences, Devi Ahilya University, Indore, India. Electronic address: hajelak@gmail.com.
authors.forename: Krishnan
authors.initials: K
authors.lastname: Hajela
mesh_terms: D000818:Animals; D001665:Binding Sites; D006041:Goats; D037601:Mannose-Binding Lectin / Q000097:blood / Q000737:chemistry / Q000378:metabolism*; D008670:Metals / Q000378:metabolism*; D011485:Protein Binding; D017434:Protein Structure, Tertiary
chemical_list: D037601:Mannose-Binding Lectin; D008670:Metals
keywords: Carbohydrate Recognition Domain; Divalent ion interactions; Electron Paramagnetic Resonance; MBL; Mannose binding lectin