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A clamp‐like orientation of basic residues set in a parallelogram is essential for heparin binding
Author(s) -
Cheng YiYun,
Cheng ChaoSheng,
Lee TianRen,
Chang WunShaing Wayne,
Lyu PingChiang
Publication year - 2016
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12361
Subject(s) - parallelogram , heparin , chemistry , biophysics , clamp , arginine , biochemistry , stereochemistry , crystallography , biology , computer science , hinge , amino acid , physics , clamping , classical mechanics , computer vision
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.