Conformational stability of the bacterial adhesin, FimH , with an inactivating mutation
Abstract
Allostery governing two conformational states is one of the proposed mechanisms for catch-bond behavior in adhesive proteins. In FimH, a catch-bond protein expressed by pathogenic bacteria, separation of two domains disrupts inhibition by the pilin domain. Thus, tensile force can induce a conformational change in the lectin domain, from an inactive state to an active state with high affinity. To better understand allosteric inhibition in...
Paper Details
Title
Conformational stability of the bacterial adhesin, FimH , with an inactivating mutation
Published Date
Oct 29, 2020
Journal
Volume
89
Issue
3
Pages
276 - 288
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