Report

Evolution of fold switching in a metamorphic protein

See allHide authors and affiliations

Science  01 Jan 2021:
Vol. 371, Issue 6524, pp. 86-90
DOI: 10.1126/science.abd8700

You are currently viewing the editor's summary.

View Full Text

Log in to view the full text

Log in through your institution

Log in through your institution

One sequence encoding two structures

Most proteins have stable, folded structures, but there are rare examples of metamorphic proteins that can switch between two different folds that may each have a different function. Dishman et al. investigated the evolution of XCL1, which is a member of the chemokine family that interconverts between the chemokine fold and a second, noncanonical fold that forms dimers. The authors used nuclear magnetic resonance spectroscopy to investigate the structures of inferred evolutionary ancestral sequences. Their results suggest that XCL1 evolved from an ancestor with the chemokine fold and then transitioned to prefer the noncanonical fold before reaching the modern-day metamorphic protein.

Science, this issue p. 86

View Full Text

Stay Connected to Science