PUBLICATION
Non-3D domain swapped crystal structure of truncated zebrafish alphaA crystallin
- Authors
- Laganowsky, A., and Eisenberg, D.
- ID
- ZDB-PUB-100730-20
- Date
- 2010
- Source
- Protein science : a publication of the Protein Society 19(10): 1978-1984 (Journal)
- Registered Authors
- Keywords
- X-ray diffraction, small heat shock protein, protein chaperone, cataract, eye lens transparency, alpha crystallin
- MeSH Terms
-
- Animals
- Cattle
- Protein Structure, Tertiary*
- Crystallography, X-Ray
- Amino Acid Sequence
- Sequence Homology, Amino Acid
- Hydrogen Bonding
- Peptide Fragments/chemistry*
- Peptide Fragments/genetics
- Models, Molecular
- Protein Conformation
- Protein Multimerization
- Zebrafish Proteins/chemistry*
- Zebrafish Proteins/genetics
- Molecular Sequence Data
- Binding Sites/genetics
- Zebrafish/genetics
- Zebrafish/metabolism
- alpha-Crystallin A Chain/chemistry*
- alpha-Crystallin A Chain/genetics
- PubMed
- 20669149 Full text @ Protein Sci.
Citation
Laganowsky, A., and Eisenberg, D. (2010) Non-3D domain swapped crystal structure of truncated zebrafish alphaA crystallin. Protein science : a publication of the Protein Society. 19(10):1978-1984.
Abstract
In previous work on truncated alpha crystallins(1), we determined crystal structures of the alpha crystallin core, a seven beta-stranded immunoglobulin-like domain, with its conserved C-terminal extension. These extensions swap into neighboring cores, forming oligomeric assemblies. The extension is palindromic in sequence, binding in either of two directions. Here we report the crystal structure of a truncated alphaA crystallin from zebrafish (Danio rerio) revealing C-terminal extensions in a non-3D domain swapped, "closed" state. The extension is quasi-palindromic, bound within its own zebrafish core domain, lying in the opposite direction to that of bovine alphaA crystallin, which is bound within an adjacent core domain (1). Our findings establish that the C-terminal extension of alpha crystallin proteins can be either 3D domain swapped or non-3D domain swapped. This duality provides another molecular mechanism for alpha crystallin proteins to maintain the polydispersity that is crucial for eye lens transparency.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping