國家衛生研究院 NHRI:Item 3990099045/1235
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    题名: Identification of hydrophobic residues critical for DPP-IV dimerization
    作者: Chien, CH;Tsai, CH;Lin, CH;Chou, CY;Chen, X
    贡献者: Division of Biotechnology and Pharmaceutical Research
    摘要: The prolyl dipeptidase DPP-IV plays diverse and important roles in cellular functions. It is a membrane-bound exoprotease involved in the proteolytic cleavage of several insulin-sensing hormones. The inhibition of its enzymatic activity has been proven effective in the treatment of type II diabetes. Homodimeric DPP-IV interacts extracellularly with adenosine deaminase, and this interaction is critical for adenosine signaling and T-cell proliferation. In this study, we investigated the contribution of hydrophobic interactions to the dimerization of DPP-IV. Hydrophobic residues F713, W734, and Y735 were found to be essential for DPP-IV dimerization. Moreover, the enzymatic activity of DPP-IV was correlated with its quaternary structure. Monomeric DPP-IV had only residual activity left, ranging from 1/30 to 1/1600 of the dimeric forms. Using a surface plasmon resonance technique, we demonstrated that the affinity of these DPP-IV monomers for adenosine deaminase was not significantly altered, compared to that of dimeric DPP-IV. The study not only identifies the hydrophobic interactions critical for DPP-IV dimer formation, but also reveals no global conformational change upon the formation of monomers as determined by the protein-protein interaction ( Kd) of DPP-IV with adenosine deaminase.
    关键词: Biochemistry & Molecular Biology
    日期: 2006-06-13
    關聯: Biochemistry. 2006 Jun;45(23):7006-7012.
    Link to: http://dx.doi.org/10.1021/bi060401c
    JIF/Ranking 2023: http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=NHRI&SrcApp=NHRI_IR&KeyISSN=0006-2960&DestApp=IC2JCR
    Cited Times(WOS): https://www.webofscience.com/wos/woscc/full-record/WOS:000238047600002
    Cited Times(Scopus): http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=33745045683
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