ePrints@IIScePrints@IISc Home | About | Browse | Latest Additions | Advanced Search | Contact | Help

Impact of glycosylation on stability, structure and unfolding of soybean agglutinin (SBA): an insight from thermal perturbation molecular dynamics simulations

Halder, Swagata and Surolia, Avadhesha and Mukhopadhyay, Chaitali (2015) Impact of glycosylation on stability, structure and unfolding of soybean agglutinin (SBA): an insight from thermal perturbation molecular dynamics simulations. In: GLYCOCONJUGATE JOURNAL, 32 (6). pp. 371-384.

[img] PDF
Gly_Jou_32-6_371_2015.pdf - Published Version
Restricted to Registered users only

Download (5MB) | Request a copy
Official URL: http://dx.doi.org/10.1007/s10719-015-9601-y

Abstract

Glycosylation has been recognized as one of the most prevalent and complex post-translational modification<Emphasis Type=''Strikethrough''>s of proteins involving numerous enzymes and substrates. Its effect on the protein conformational transitions is not clearly understood yet. In this study, we have examined the effect of glycosylation on protein stability using molecular dynamics simulation of legume lectin soybean agglutinin (SBA). Its glycosylated moiety consists of high mannose type N-linked glycan (Man(9)GlcNAc(2)). To unveil the structural perturbations during thermal unfolding of these two forms, we have studied and compared them to the experimental results. From the perspective of dynamics, our simulations revealed that the nonglycosylated monomeric form is less stable than corresponding glycosylated form at normal and elevated temperatures. Moreover, at elevated temperature thermal destabilization is more prominent in solvent exposed loops, turns and ends of distinct beta sheets. SBA maintains it folded structure due to some important saltbridges, hydrogen bonds and hydrophobic interactions within the protein. The reducing terminal GlcNAc residues interact with the protein residues VAL161, PRO182 and SER225 via hydrophobic and via hydrogen bonding with ASN 9 and ASN 75. Our simulations also revealed that single glycosylation (ASN75) has no significant effect on corresponding cis peptide angle orientation. This atomistic description might have important implications for understanding the functionality and stability of Soybean agglutinin.

Item Type: Journal Article
Publication: GLYCOCONJUGATE JOURNAL
Publisher: SPRINGER
Additional Information: Copy right for this article belongs to the SPRINGER, VAN GODEWIJCKSTRAAT 30, 3311 GZ DORDRECHT, NETHERLANDS
Keywords: Soybean agglutinin; Lectin; Glycosylation; Protein unfolding; Molecular dynamics simulations
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited: 26 Aug 2015 05:40
Last Modified: 26 Aug 2015 05:40
URI: http://eprints.iisc.ac.in/id/eprint/52237

Actions (login required)

View Item View Item