University of Sussex
Browse

File(s) not publicly available

Reconciling the lock-and-key and dynamic views of canonical serine protease inhibitor action

journal contribution
posted on 2023-06-07, 22:31 authored by Peter Varnai, Zoltan Gáspári, Balazs Szappanos, Andras Perczel
The efficiency of canonical serine protease inhibitors is conventionally attributed to the rigidity of their protease binding loop with no conformational change upon enzyme binding, yielding an example of the lock-and-key model for biomolecular interactions. However, solution-state structural studies revealed considerable flexibility in their protease binding loop. We resolve this apparent contradiction by showing that enzyme binding of small, 35-residue inhibitors is actually a dynamic conformer selection process on the nanosecond-timescale. Thus, fast timescale dynamics enables the association rate to be solely diffusion-controlled just like in the rigid-body model.

History

Publication status

  • Published

Journal

FEBS Letters

ISSN

0014-5793

Publisher

Elsevier

Issue

1

Volume

584

Page range

203-206

Pages

4.0

Department affiliated with

  • Chemistry Publications

Full text available

  • No

Peer reviewed?

  • Yes

Legacy Posted Date

2012-02-06

Usage metrics

    University of Sussex (Publications)

    Categories

    No categories selected

    Exports

    RefWorks
    BibTeX
    Ref. manager
    Endnote
    DataCite
    NLM
    DC