| Autor: |
Kerry M, Goodman, Rotem, Rubinstein, Hanbin, Dan, Fabiana, Bahna, Seetha, Mannepalli, Göran, Ahlsén, Chan, Aye Thu, Rosemary V, Sampogna, Tom, Maniatis, Barry, Honig, Lawrence, Shapiro |
| Rok vydání: |
2017 |
| Předmět: |
|
| Zdroj: |
Proceedings of the National Academy of Sciences of the United States of America. 114(46) |
| ISSN: |
1091-6490 |
| Popis: |
Pcdhs are cell surface homophilic recognition proteins expressed stochastically to assign individual identities to each neuron. These individual identities ensure repulsion between neurites from the same cell and ensure that neurites from different cells do not repel. However, it is difficult to understand how only ∼60 Pcdh isoforms can provide sufficient diversity for the billions of neurons in vertebrate nervous systems. Here, we report the crystal structure of a Pcdh cis-dimer through which individual Pcdh isoforms associate to form diverse bivalent recognition units. The structure reveals asymmetry in the cis-dimer interaction and suggests restrictions on isoform combinations compatible with cis-dimerization. These findings provide a framework to understand Pcdh cis-dimerization and the compositions of functional repertoires of Pcdh recognition units. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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