title: Protein production, crystallization and preliminary crystallographic analysis of the four N-terminal immunoglobulin domains of Down syndrome cell adhesion molecule 1.
abstract: Down syndrome cell adhesion molecule 1 (Dscam1), a member of the immunoglobulin (Ig) superfamily, plays important roles in both the nervous and the immune systems. Via alternative RNA splicing, Drosophila Dscam1 encodes a vast family of Ig-containing proteins that exhibit isoform-specific homophilic binding. Whether different Dscam1 isoforms adopt the same dimerization mode is under debate, and the detailed mechanism of Dscam1 specificity remains unclear. In this study, eight different isforms of Dscam1 Ig1-4 have been cloned, overexpressed, purified to homogeneity and crystallized. X-ray data were collected to 1.9-4.0 Å resolution. These structures will provide the opportunity to perform extensive structural comparisons of different Dscam1 isoforms and provide insight into its specificity.
authors.affiliation: State Key Laboratory of Biotherapy and Cancer Center, West China Hospital, Sichuan University and Collaborative Innovation Center of Biotherapy, Chengdu 610041, People's Republic of China.
authors.forename: Linna
authors.initials: L
authors.lastname: Cheng
authors.affiliation: State Key Laboratory of Biotherapy and Cancer Center, West China Hospital, Sichuan University and Collaborative Innovation Center of Biotherapy, Chengdu 610041, People's Republic of China.
authors.forename: Shu Ang
authors.initials: SA
authors.lastname: Li
authors.forename: Jia-huai
authors.initials: JH
authors.lastname: Wang
authors.affiliation: State Key Laboratory of Biotherapy and Cancer Center, West China Hospital, Sichuan University and Collaborative Innovation Center of Biotherapy, Chengdu 610041, People's Republic of China.
authors.forename: Yamei
authors.initials: Y
authors.lastname: Yu
authors.affiliation: State Key Laboratory of Biotherapy and Cancer Center, West China Hospital, Sichuan University and Collaborative Innovation Center of Biotherapy, Chengdu 610041, People's Republic of China.
authors.forename: Qiang
authors.initials: Q
authors.lastname: Chen
mesh_terms: D000818:Animals; D016367:Baculoviridae / Q000235:genetics / Q000378:metabolism; D015815:Cell Adhesion Molecules; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D029721:Drosophila Proteins / Q000737:chemistry* / Q000235:genetics; D004331:Drosophila melanogaster / Q000737:chemistry* / Q000276:immunology / Q000378:metabolism; D015870:Gene Expression; D005810:Multigene Family; D019006:Neural Cell Adhesion Molecules / Q000737:chemistry* / Q000235:genetics; D020033:Protein Isoforms / Q000737:chemistry / Q000235:genetics; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D061987:Sf9 Cells; D018411:Spodoptera; D014961:X-Ray Diffraction
chemical_list: D015815:Cell Adhesion Molecules; D029721:Drosophila Proteins; C491736:Dscam1 protein, Drosophila; D019006:Neural Cell Adhesion Molecules; D020033:Protein Isoforms; D011994:Recombinant Proteins
keywords: Dscam1; RNA splicing; crystallization; homophilic dimer; horseshoe configuration