4ZPS

Crystal Structure of Protocadherin Gamma A8 EC1-3

4ZPS の概要

• エントリーDOI: 10.2210/pdb4zps/pdb
• 関連するPDBエントリー: 4ZPL 4ZPM 4ZPN 4ZPO 4ZPP 4ZPQ
• 分子名称: MCG133388, isoform CRA_m, alpha-D-mannopyranose, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: cell adhesion
• 由来する生物種: Mus musculus (Mouse)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 36429.89

構造登録者

Goodman, K.M.,Mannepalli, S.,Shapiro, L. (登録日: 2015-05-08, 公開日: 2015-10-28, 最終更新日: 2024-11-06)

主引用文献

Rubinstein, R.,Thu, C.A.,Goodman, K.M.,Wolcott, H.N.,Bahna, F.,Mannepalli, S.,Ahlsen, G.,Chevee, M.,Halim, A.,Clausen, H.,Maniatis, T.,Shapiro, L.,Honig, B.
Molecular Logic of Neuronal Self-Recognition through Protocadherin Domain Interactions.
Cell, 163:629-642, 2015

PubMed Abstract: Self-avoidance, a process preventing interactions of axons and dendrites from the same neuron during development, is mediated in vertebrates through the stochastic single-neuron expression of clustered protocadherin protein isoforms. Extracellular cadherin (EC) domains mediate isoform-specific homophilic binding between cells, conferring cell recognition through a poorly understood mechanism. Here, we report crystal structures for the EC1-EC3 domain regions from four protocadherin isoforms representing the α, β, and γ subfamilies. All are rod shaped and monomeric in solution. Biophysical measurements, cell aggregation assays, and computational docking reveal that trans binding between cells depends on the EC1-EC4 domains, which interact in an antiparallel orientation. We also show that the EC6 domains are required for the formation of cis-dimers. Overall, our results are consistent with a model in which protocadherin cis-dimers engage in a head-to-tail interaction between EC1-EC4 domains from apposed cell surfaces, possibly forming a zipper-like protein assembly, and thus providing a size-dependent self-recognition mechanism.

PubMed: 26478182
DOI: 10.1016/j.cell.2015.09.026

実験手法

X-RAY DIFFRACTION (2.9 Å)