Protein production, crystallization and preliminary X-ray analysis of two isoforms of the Dscam1 Ig7 domain
Copyright policy )Protein production, crystallization and preliminary X-ray analysis of two isoforms of the Dscam1 Ig7 domain
DrosophilaDown syndrome cell adhesion molecule 1 (Dscam1) plays a critical role in neural development. It can potentially form 38 016 isoforms through alternative RNA splicing, and exhibits isoform-specific homophilic interaction through three variable Ig domains (Ig2, Ig3 and Ig7). The diversity and homophilic interaction are essential for its functions. Ig7 has 33 isoforms and is the most variable among the three variable Ig domains. However, only one isoform of Ig7 (isoform 30) has been structurally determined to date. Here, two isoforms of Dscam1 Ig7 (isoforms 5 and 9; Ig75and Ig79) were produced and crystallized. Diffraction data from Ig75and Ig79crystals were processed to resolutions of 1.95 and 2.37 Å, respectively. Comparison of different Dscam1 Ig7 isoforms will provide insight into the mechanism of its binding specificity.
- State Key Laboratory of Biotherapy China (People's Republic of)
- Sichuan University China (People's Republic of)
Crystallography, X-Ray, Protein Structure, Tertiary, Drosophila melanogaster, Escherichia coli, Animals, Drosophila Proteins, Protein Isoforms, Crystallization, Cell Adhesion Molecules, Neural Cell Adhesion Molecules
Crystallography, X-Ray, Protein Structure, Tertiary, Drosophila melanogaster, Escherichia coli, Animals, Drosophila Proteins, Protein Isoforms, Crystallization, Cell Adhesion Molecules, Neural Cell Adhesion Molecules
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