國家衛生研究院 NHRI:Item 3990099045/9207
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    题名: Structure of human collapsin response mediator protein 1: A possible role of its C-terminal tail
    作者: Liu, SH;Huang, SF;Hsu, YL;Pan, SH;Chen, YJ;Lin, YH
    贡献者: National Institute of Cancer Research
    摘要: Collapsin response mediator protein 1 (CRMP-1) is the first identified member of the CRMP family and is crucial for both the mediation of neuronal differentiation and in suppressing the invasion of lung cancer. The crystal structure of full-length human CRMP-1 was determined at a resolution of 3 Å. Human CRMP-1 comprises a tetrameric assembly; its overall structure is similar to that of mouse CRMP-1, but the measured electron density of the C-terminal residues 488-496 show a randomly coiled link that connects the protomers to each other, within which residues 497-572 are proteolytically susceptible in vivo. Deletion of residues 472-572 by thrombin in vitro not only releases a randomly coiled tail but also transduces observable structural changes of CRMP-1, as revealed by analytical size-exclusive chromatography and circular dichroism spectra. These results indicate a possible alternative role in CRMP dynamics and function.
    日期: 2015-08
    關聯: Acta Crystallographica Section:F Structural Biology Communications. 2015 Aug;71:938-945.
    Link to: http://dx.doi.org/10.1107/S2053230X15009243
    JIF/Ranking 2023: http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=NHRI&SrcApp=NHRI_IR&KeyISSN=2053-230X&DestApp=IC2JCR
    Cited Times(WOS): https://www.webofscience.com/wos/woscc/full-record/WOS:000359352700002
    Cited Times(Scopus): http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=84938902082
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