Ion mobility mass spectrometry measures the conformational landscape of p27 and its domains and how this is modulated upon interaction with Cdk2/cyclin A

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Beveridge, Rebecca and Migas, Lukasz G. and Kriwacki, Richard W. and Barran, Perdita E. (2019) Ion mobility mass spectrometry measures the conformational landscape of p27 and its domains and how this is modulated upon interaction with Cdk2/cyclin A. Angewandte Chemie International Edition, 58 (10). 3114—3118. ISSN 1521-3773 (https://doi.org/10.1002/anie.201812697)

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Abstract

Intrinsically disordered proteins have been reported to undergo disorder‐to‐order transitions upon binding to their partners in the cell. The extent of the ordering upon binding and the lack of order prior to binding is difficult to visualize with classical structure determination methods. Binding of p27 to the Cdk2/cyclin A complex is accompanied by partial folding of p27 in the KID domain, with the retention of dynamic behavior for function, particularly in the C‐terminal half of the protein. Herein, native ion mobility mass spectrometry (IM‐MS) is employed to measure the intrinsic dynamic properties of p27, both in isolation and within the trimeric complex with Cdk2/cyclin A. The trimeric Cdk2/cyclin A/p27‐KID complex possesses significant structural heterogeneity compared to Cdk2/cyclin A. These findings support the formation of a fuzzy complex in which both the N‐ and C‐termini of p27 interact with Cdk2/cyclin A in multiple, closely associated states.

ORCID iDs

Beveridge, Rebecca ORCID logoORCID: https://orcid.org/0000-0003-0320-6496, Migas, Lukasz G., Kriwacki, Richard W. and Barran, Perdita E.;
  • Item type:Article
    ID code:72712
    Dates:
    Date
    Event
    4 March 2019
    Published
    24 January 2019
    Published Online
    20 December 2018
    Accepted
    Subjects:Science > Chemistry
    Department:Faculty of Science > Pure and Applied Chemistry
    Depositing user: Pure Administrator
    Date deposited:11 Jun 2020 12:24
    Last modified:20 Dec 2024 01:50
    URI:https://strathprints.strath.ac.uk/id/eprint/72712
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