Divalent metal ions binding properties of goat serum mannose binding lectin

Pankaj Kumar Patel; Maliram Hindala; Bavita Kohli; Krishnan Hajela

doi:10.1016/j.ijbiomac.2015.06.049

Divalent metal ions binding properties of goat serum mannose binding lectin

Int J Biol Macromol. 2015 Sep:80:324-7. doi: 10.1016/j.ijbiomac.2015.06.049. Epub 2015 Jun 28.

Authors

Pankaj Kumar Patel¹, Maliram Hindala¹, Bavita Kohli², Krishnan Hajela³

Affiliations

¹ School of Life Sciences, Devi Ahilya University, Indore, India.
² School of Life Sciences, Devi Ahilya University, Indore, India; Department of Bio-Technology, ISLE, IPS Academy, Indore, India.
³ School of Life Sciences, Devi Ahilya University, Indore, India. Electronic address: hajelak@gmail.com.

PMID: 26126945
DOI: 10.1016/j.ijbiomac.2015.06.049

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.

Keywords: Carbohydrate Recognition Domain; Divalent ion interactions; Electron Paramagnetic Resonance; MBL; Mannose binding lectin.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Animals
Binding Sites
Goats
Mannose-Binding Lectin / blood
Mannose-Binding Lectin / chemistry
Mannose-Binding Lectin / metabolism*
Metals / metabolism*
Protein Binding
Protein Structure, Tertiary

Substances

Mannose-Binding Lectin
Metals