國家衛生研究院 NHRI:Item 3990099045/9955
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    Please use this identifier to cite or link to this item: http://ir.nhri.org.tw/handle/3990099045/9955


    Title: A clamp-like orientation of basic residues set in a parallelogram is essential for heparin binding
    Authors: Cheng, YY;Cheng, CS;Lee, TR;Chang, WW;Lyu, PC
    Contributors: National Institute of Cancer Research
    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 beta-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 ~5A with ~100 degrees interior angle is advantageous for high heparin affinity.
    Date: 2016-09
    Relation: FEBS Letters. 2016 Sep;590(18):3089-3097.
    Link to: http://dx.doi.org/10.1002/1873-3468.12361
    JIF/Ranking 2023: http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=NHRI&SrcApp=NHRI_IR&KeyISSN=0014-5793&DestApp=IC2JCR
    Cited Times(WOS): https://www.webofscience.com/wos/woscc/full-record/WOS:000384807700005
    Cited Times(Scopus): http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=84984710616
    Appears in Collections:[Wun-Shaing Wayne Chang] Periodical Articles

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