PUBLICATION
Crystallization and preliminary X-ray diffraction analysis of the two distinct types of zebrafish β2-microglobulin
- Authors
- Chen, Z., Zhang, N., Lu, S., Tariq, M., Wang, J., Xia, C.
- ID
- ZDB-PUB-150610-1
- Date
- 2015
- Source
- Acta crystallographica. Section F, Structural biology communications 71: 794-798 (Journal)
- Registered Authors
- Keywords
- MHC class I, zebrafish, β2-microglobulin
- MeSH Terms
-
- Amino Acid Sequence
- Animals
- Cloning, Molecular
- Crystallization
- Crystallography, X-Ray
- Escherichia coli/genetics
- Escherichia coli/metabolism
- Fish Proteins/chemistry*
- Fish Proteins/genetics
- Fish Proteins/immunology
- Gene Expression
- Major Histocompatibility Complex
- Molecular Sequence Data
- Protein Isoforms/chemistry
- Protein Isoforms/genetics
- Protein Isoforms/immunology
- Recombinant Proteins/chemistry
- Recombinant Proteins/genetics
- Recombinant Proteins/immunology
- Sequence Alignment
- X-Ray Diffraction
- Zebrafish/genetics*
- Zebrafish/immunology
- beta 2-Microglobulin/chemistry*
- beta 2-Microglobulin/genetics
- beta 2-Microglobulin/immunology
- PubMed
- 26057815 Full text @ Acta Crystallogr F Struct Biol Commun
Citation
Chen, Z., Zhang, N., Lu, S., Tariq, M., Wang, J., Xia, C. (2015) Crystallization and preliminary X-ray diffraction analysis of the two distinct types of zebrafish β2-microglobulin. Acta crystallographica. Section F, Structural biology communications. 71:794-798.
Abstract
β2-Microglobulin (β2m) noncovalently associates with the heavy chain of major histocompatibility complex class I (MHC I) molecules, which bind foreign antigen peptides to control the cytotoxic T lymphocyte (CTL) immune response. In contrast to mammals, there are distinct types of β2ms derived from two loci in a number of teleost species. In order to clarify the structures of the β2ms, the zebrafish (Danio rerio) β2ms Dare-β2m-I and Dare-β2m-II were expressed in Escherichia coli, purified and crystallized, and diffraction data were collected to 1.6 and 1.9 Å resolution, respectively. Both crystals belonged to space group P212121. The unit-cell parameters were determined to be a = 38.2, b = 50.4, c = 50.9 Å for Dare-β2m-I and a = 38.9, b = 52.7, c = 65.8 Å for Dare-β2m-II. Each asymmetric unit was constituted of one molecule, with Matthews coefficients of 2.22 and 3.01 Å(3) Da(-1) and solvent contents of 45 and 59% for Dare-β2m-I and Dare-β2m-II, respectively. These two β2m structures will provide relevant information for further studies of the structures of the MHC I complex.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping