PUBLICATION
The centriolar protein CPAP G-box: an amyloid fibril in a single domain
- Authors
- Cutts, E.E., Inglis, A., Stansfeld, P.J., Vakonakis, I., Hatzopoulos, G.N.
- ID
- ZDB-PUB-170214-86
- Date
- 2015
- Source
- Biochemical Society transactions 43: 838-43 (Journal)
- Registered Authors
- Keywords
- CPAP, b-sheet, centriole, fibril, structure
- MeSH Terms
-
- Amyloid/chemistry
- Amyloid/metabolism
- Animals
- Centrioles/chemistry*
- Centrioles/metabolism
- Drosophila Proteins/chemistry*
- Drosophila Proteins/genetics
- Drosophila Proteins/metabolism
- Humans
- Microtubule-Associated Proteins/chemistry*
- Microtubule-Associated Proteins/genetics
- Microtubule-Associated Proteins/metabolism
- Models, Molecular*
- Mutation
- Protein Aggregation, Pathological/metabolism
- Protein Aggregation, Pathological/pathology*
- Protein Conformation
- Protein Folding
- Protein Stability
- Protein Structure, Secondary
- Protein Structure, Tertiary
- Structural Homology, Protein
- Zebrafish Proteins/chemistry*
- Zebrafish Proteins/genetics
- Zebrafish Proteins/metabolism
- PubMed
- 26517891 Full text @ Biochem Soc. Trans.
Citation
Cutts, E.E., Inglis, A., Stansfeld, P.J., Vakonakis, I., Hatzopoulos, G.N. (2015) The centriolar protein CPAP G-box: an amyloid fibril in a single domain. Biochemical Society transactions. 43:838-43.
Abstract
Centrioles are evolutionarily conserved cylindrical cell organelles with characteristic radial symmetry. Despite their considerable size (400 nm × 200 nm, in humans), genetic studies suggest that relatively few protein components are involved in their assembly. We recently characterized the molecular architecture of the centrosomal P4.1-associated protein (CPAP), which is crucial for controlling the centriolar cylinder length. Here, we review the remarkable architecture of the C-terminal domain of CPAP, termed the G-box, which comprises a single, entirely solvent exposed, antiparallel β-sheet. Molecular dynamics simulations support the stability of the G-box domain even in the face of truncations or amino acid substitutions. The similarity of the G-box domain to amyloids (or amyloid precursors) is strengthened by its oligomeric arrangement to form continuous fibrils. G-box fibrils were observed in crystals as well as in solution and are also supported by simulations. We conclude that the G-box domain may well represent the best analogue currently available for studies of exposed β-sheets, unencumbered by additional structural elements or severe aggregations problems.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping