5DZW

Protocadherin alpha 4 extracellular cadherin domains 1-4

5DZW の概要

• エントリーDOI: 10.2210/pdb5dzw/pdb
• 関連するPDBエントリー: 5DZV 5DZX 5DZY
• 分子名称: Protocadherin alpha-4, alpha-D-mannopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• 機能のキーワード: cadherin, dimer, extracellular, cell adhesion
• 由来する生物種: Mus musculus (Mouse)
• 細胞内の位置: Cell membrane ; Single-pass type I membrane protein : O88689
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 48742.78

構造登録者

Goodman, K.M.,Bahna, F.,Mannepalli, S.,Honig, B.,Shapiro, L. (登録日: 2015-09-26, 公開日: 2016-05-04, 最終更新日: 2024-10-23)

主引用文献

Goodman, K.M.,Rubinstein, R.,Thu, C.A.,Bahna, F.,Mannepalli, S.,Ahlsen, G.,Rittenhouse, C.,Maniatis, T.,Honig, B.,Shapiro, L.
Structural Basis of Diverse Homophilic Recognition by Clustered alpha- and beta-Protocadherins.
Neuron, 90:709-723, 2016

PubMed Abstract: Clustered protocadherin proteins (α-, β-, and γ-Pcdhs) provide a high level of cell-surface diversity to individual vertebrate neurons, engaging in highly specific homophilic interactions to mediate important roles in mammalian neural circuit development. How Pcdhs bind homophilically through their extracellular cadherin (EC) domains among dozens of highly similar isoforms has not been determined. Here, we report crystal structures for extracellular regions from four mouse Pcdh isoforms (α4, α7, β6, and β8), revealing a canonical head-to-tail interaction mode for homophilic trans dimers comprising primary intermolecular EC1:EC4 and EC2:EC3 interactions. A subset of trans interface residues exhibit isoform-specific conservation, suggesting roles in recognition specificity. Mutation of these residues, along with trans-interacting partner residues, altered the specificities of Pcdh interactions. Together, these data show how sequence variation among Pcdh isoforms encodes their diverse strict homophilic recognition specificities, which are required for their key roles in neural circuit assembly.

PubMed: 27161523
DOI: 10.1016/j.neuron.2016.04.004

実験手法

X-RAY DIFFRACTION (2.43 Å)