AI Article Synopsis
- Most studies have looked at the biological functions of heparin-binding proteins, but information on their key interacting residues and structures is limited.
- This research used a mini version of the Streptococcal protein G to explore how specific positively charged residues in a β-sheet shape enhance heparin binding.
- The findings revealed that a clamp-like arrangement of spaced-out basic residues, with particular angular positioning, is beneficial for strong heparin attraction.
Article Abstract
While the majority of studies have focused on the biological roles of heparin-binding proteins, relatively little is known about their key residues and structural elements responsible for heparin interaction. In this study, we employed the IgG-binding domain B1 of Streptococcal protein G as a miniature scaffold to investigate how certain positively charged residues within the β-sheet conformation become favorable for heparin binding. By performing a series of arginine substitution mutations followed by gain-of-heparin-binding analysis, we deduced that a clamp-like orientation with discontinuous basic residues separated by ~ 5 Å with ~ 100° interior angle is advantageous for high heparin affinity.
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| http://dx.doi.org/10.1002/1873-3468.12361 | DOI Listing |
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