Amyloid-like fibrils of ribonuclease A with three-dimensional domain-swapped and native-like structure

Shilpa Sambashivan, Yanshun Liu, Michael R. Sawaya, Mari Gingery and David Eisenberg ()
Additional contact information
Shilpa Sambashivan: Howard Hughes Medical Institute, UCLA-DOE Institute for Genomics and Proteomics, UCLA
Yanshun Liu: Howard Hughes Medical Institute, UCLA-DOE Institute for Genomics and Proteomics, UCLA
Michael R. Sawaya: Howard Hughes Medical Institute, UCLA-DOE Institute for Genomics and Proteomics, UCLA
Mari Gingery: Howard Hughes Medical Institute, UCLA-DOE Institute for Genomics and Proteomics, UCLA
David Eisenberg: Howard Hughes Medical Institute, UCLA-DOE Institute for Genomics and Proteomics, UCLA

Nature, 2005, vol. 437, issue 7056, 266-269

Abstract: Prions: form and infectivity The prospects of limiting the spread of transmissible spongiform encephalopathies such as Creutzfeldt–Jakob disease depend in part on identifying the most infectious forms of the prions that carry the diseases. A study of modified scrapie prions shows that clusters of 14 to 28 prion proteins are the most infectious and that clusters of less than six molecules have virtually no infectivity. That could have implications for the treatment of diseases such as Alzheimer's and Parkinson's, characterized by deposition of prion-related amyloid fibrils. It's possible that efforts to alleviate symptoms by destabilizing these large protein aggregates might make things worse by producing smaller, more infective particles. Two other papers in this issue tackle fundamental aspects of the biology of prions and amyloid fibrils. The conversion of the yeast protein Sup35 to its prion form does not need to happen during the synthesis of Sup35 — mature and fully functional molecules can readily join a prion seed. This remodelling of the mature protein is accompanied by the immediate loss of its activity. And a study of a ‘designed’ amyloid fibril made from ribonuclease A reveals that amyloid containing native-like molecules can retain enzyme activity. This involves a domain swap with the neighbouring protein, and supports the ‘zipper-spine model’ for β-amyloid structures.

Date: 2005
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/nature03916 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:437:y:2005:i:7056:d:10.1038_nature03916

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/nature03916

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().