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

Zoltán Gáspári, Péter Várnai, Balázs Szappanos, András Perczel

Research output: Article

18 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)203-206
Number of pages4
JournalFEBS letters
Volume584
Issue number1
DOIs
Publication statusPublished - jan. 4 2010

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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