Structural and binding studies of SAP-1 protein with heparin.

Journal article


Yadav, V. 2014. Structural and binding studies of SAP-1 protein with heparin. Chemical biology & drug design. Vol 85 (Issue 3), pp. 404 - 410. https://doi.org/10.1111/cbdd.12420
AuthorsYadav, V.
Abstract

SAP-1 is a low molecular weight cysteine protease inhibitor (CPI) which belongs to type-2 cystatins family. SAP-1 protein purified from human seminal plasma (HuSP) has been shown to inhibit cysteine and serine proteases and exhibit interesting biological properties, including high temperature and pH stability. Heparin is a naturally occurring glycosaminoglycan (with varied chain length) which interacts with a number of proteins and regulates multiple steps in different biological processes. As an anticoagulant, heparin enhances inhibition of thrombin by the serpin antithrombin III. Therefore, we have employed surface plasmon resonance (SPR) to improve our understanding of the binding interaction between heparin and SAP-1 (protease inhibitor). SPR data suggest that SAP-1 binds to heparin with a significant affinity (KD = 158 nm). SPR solution competition studies using heparin oligosaccharides showed that the binding of SAP-1 to heparin is dependent on chain length. Large oligosaccharides show strong binding affinity for SAP-1. Further to get insight into the structural aspect of interactions between SAP-1 and heparin, we used modelled structure of the SAP-1 and docked with heparin and heparin-derived polysaccharides. The results suggest that a positively charged residue lysine plays important role in these interactions. Such information should improve our understanding of how heparin, present in the reproductive tract, regulates cystatins activity.

KeywordsBinding affinity; ; Cystatins; ; Heparin; ; Key residues; ; Molecular docking; ; Surface plasmon resonance
Year2014
JournalChemical biology & drug design
Journal citationVol 85 (Issue 3), pp. 404 - 410
PublisherJohn Wiley & Sons Ltd
ISSN17470277
1747-0285
Digital Object Identifier (DOI)https://doi.org/10.1111/cbdd.12420
Web address (URL)https://doi.org/10.1111/cbdd.12420
Output statusPublished
Publication dates
Online21 Aug 2014
Online22 Sep 2014
Online12 Feb 2015
Publication process dates
Accepted13 Aug 2014
Deposited15 Jun 2023
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