Structural and functional analysis of cystatin E reveals enzymologically relevant dimer and amyloid fibril states
Volume: 293, Issue: 34, Pages: 13151 - 13165
Published: Aug 1, 2018
Abstract
Protein activity is often regulated by altering the oligomerization state. One mechanism of multimerization involves domain swapping, wherein proteins exchange parts of their structures and thereby form long-lived dimers or multimers. Domain swapping has been specifically observed in amyloidogenic proteins, for example the cystatin superfamily of cysteine protease inhibitors. Cystatins are twin-headed inhibitors, simultaneously targeting the...
Paper Details
Title
Structural and functional analysis of cystatin E reveals enzymologically relevant dimer and amyloid fibril states
Published Date
Aug 1, 2018
Volume
293
Issue
34
Pages
13151 - 13165
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