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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Cheng YY,Cheng CS,Lee TR,Chang WS,Lyu PCdoi
10.1002/1873-3468.12361subject
Has Abstractpub_date
2016-09-01 00:00:00pages
3089-97issue
18eissn
0014-5793issn
1873-3468journal_volume
590pub_type
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