Structural basis of Dscam1 homodimerization: Insights into context constraint for protein recognition

• Published in: Science advances Vol. 2; no. 5; p. e1501118
• Main Authors: Li, Shu-Ang, Cheng, Linna, Yu, Yamei, Wang, Jia-huai, Chen, Qiang
• Format: Journal Article
• Language: English
• Published: United States AAAS 01.05.2016; American Association for the Advancement of Science
• Subjects: Alternative Splicing; Amino Acid Sequence; Drosophila Proteins - chemistry; Drosophila Proteins - genetics; Drosophila Proteins - metabolism; Glycosylation; Models, Molecular; Neural Cell Adhesion Molecules - chemistry; Neural Cell Adhesion Molecules - genetics; Neural Cell Adhesion Molecules - metabolism; Protein Binding; Protein Conformation; Protein Isoforms; Protein Multimerization; SciAdv r-articles; Static Electricity; Structural Biology; protein recognition; crystal structure; Dscam1; RNA splicing; homodimer

Comparison of Dscam1 structures reveals the detailed mechanism of Dscam1 isoform-specific recognition. The Drosophila neural receptor Dscam1 (Down syndrome cell adhesion molecule 1) plays an essential role in neuronal wiring and self-avoidance. Dscam1 potentially encodes 19,008 ectodomains through a...