Ontology highlight
ABSTRACT:
SUBMITTER: Yoshizumi A
PROVIDER: S-EPMC3093825 | biostudies-literature | 2011 May
REPOSITORIES: biostudies-literature
Yoshizumi Ayumi A Fletcher Jordan M JM Yu Zhuoxin Z Persikov Anton V AV Bartlett Gail J GJ Boyle Aimee L AL Vincent Thomas L TL Woolfson Derek N DN Brodsky Barbara B
The Journal of biological chemistry 20110328 20
Collagen triple helices fold slowly and inefficiently, often requiring adjacent globular domains to assist this process. In the Streptococcus pyogenes collagen-like protein Scl2, a V domain predicted to be largely α-helical, occurs N-terminal to the collagen triple helix (CL). Here, we replace this natural trimerization domain with a de novo designed, hyperstable, parallel, three-stranded, α-helical coiled coil (CC), either at the N terminus (CC-CL) or the C terminus (CL-CC) of the collagen doma ...[more]