Structural basis of Dscam1 homodimerization: Insights into context constraint for protein recognition-Reference-Cited by-同舟云学术

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

Published:2016-05-06 Issue:5 Volume:2 Page:
ISSN:2375-2548
Container-title:Science Advances
language:en
Short-container-title:Sci. Adv.

Author:

Li Shu-Ang¹^ORCID,Cheng Linna¹,Yu Yamei¹,Wang Jia-huai²,Chen Qiang¹^ORCID

Affiliation:

1. State Key Laboratory of Biotherapy and Cancer Center, West China Hospital, Sichuan University, and Collaborative Innovation Center of Biotherapy, Chengdu 610041, P. R. China.

2. Departments of Medical Oncology and Cancer Biology, Dana-Farber Cancer Institute, Boston, MA 02215, USA. Department of Pediatrics and Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.

Abstract

Comparison of Dscam1 structures reveals the detailed mechanism of Dscam1 isoform-specific recognition.

Funder

Sichuan University

National Natural Science Foundation of China

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference33 articles.

1. Drosophila Dscam Is an Axon Guidance Receptor Exhibiting Extraordinary Molecular Diversity

2. A vast repertoire of Dscam binding specificities arises from modular interactions of variable Ig domains;Wojtowicz W. M.;Cell,2007