The Spiniest Aspect Of Amyloid Formation

The accepted paradigm has been that native proteins undergo wholesale refolding into a generic amyloid structure. Using a 'designer' enzyme that can form amyloids, Eisenberg and his team now show that this model might need modifying. The enzyme simply opens, and the amyloid spine forms from one segment of its polypeptide chain while the core of the protein remains folded. The one polypeptide segment missing after opening can be complemented - through a domain-swap with the neighbouring protein - to form active enzyme again.

"Because of their large size and variable length, amyloid fibres confound traditional methods used to determine protein structure. Sambashivan et al. use an ingenious approach to show that the protein in the fibre has a native structure," writes Andrew Miranker in a related News and Views piece.

CONTACT:

David Eisenberg (UCLA, Los Angeles, CA, USA)
Tel: +1 310 825 3754; E-mail: david@mbi.ucla.edu

Andrew Miranker (Yale University, New Haven, CT, USA)
Tel: +1 203 432 8954; E-mail: andrew.miranker@yale.edu

(C) Nature press release.

Message posted by: Trevor M. D'Souza