What makes functional amyloids work?
Crit Rev Biochem Mol Biol
; 57(4): 399-411, 2022 08.
Article
in En
| MEDLINE
| ID: mdl-35997712
ABSTRACT
Although first described in the context of disease, cross-ß (amyloid) fibrils have also been found as functional entities in all kingdoms of life. However, what are the specific properties of the cross-ß fibril motif that convey biological function, make them especially suited for their particular purpose, and distinguish them from other fibrils found in biology? This review approaches these questions by arguing that cross-ß fibrils are highly periodic, stable, and self-templating structures whose formation is accompanied by substantial conformational change that leads to a multimerization of their core and framing sequences. A discussion of each of these properties is followed by selected examples of functional cross-ß fibrils that show how function is usually achieved by leveraging many of these properties.
Key words
Full text:
1
Database:
MEDLINE
Main subject:
Amyloid
Language:
En
Journal:
Crit Rev Biochem Mol Biol
Journal subject:
BIOLOGIA MOLECULAR
/
BIOQUIMICA
Year:
2022
Type:
Article
Affiliation country:
United States