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Protein production, crystallization and preliminary X‐ray analysis of two isoforms of the Dscam1 Ig7 domain
Author(s) -
Li ShuAng,
Cheng Linna,
Yu Yamei,
Chen Qiang
Publication year - 2015
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x15002897
Subject(s) - gene isoform , crystallization , domain (mathematical analysis) , production (economics) , focus (optics) , crystallography , chemistry , biochemistry , physics , mathematics , optics , gene , mathematical analysis , macroeconomics , organic chemistry , economics
Drosophila Down 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; Ig7 5 and Ig7 9 ) were produced and crystallized. Diffraction data from Ig7 5 and Ig7 9 crystals 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.