5K8R

Structure of human clustered protocadherin gamma B3 EC1-4

5K8R の概要

• エントリーDOI: 10.2210/pdb5k8r/pdb
• 分子名称: Protocadherin gamma-B3, CALCIUM ION, CHLORIDE ION, ... (7 entities in total)
• 機能のキーワード: clustered protocadherin, protocadherin, cell adhesion
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 46555.02

構造登録者

Nicoludis, J.M.,Vogt, B.E.,Gaudet, R. (登録日: 2016-05-30, 公開日: 2016-08-24, 最終更新日: 2024-11-20)

主引用文献

Nicoludis, J.M.,Vogt, B.E.,Green, A.G.,Scharfe, C.P.,Marks, D.S.,Gaudet, R.
Antiparallel protocadherin homodimers use distinct affinity- and specificity-mediating regions in cadherin repeats 1-4.
Elife, 5:-, 2016

PubMed Abstract: Protocadherins (Pcdhs) are cell adhesion and signaling proteins used by neurons to develop and maintain neuronal networks, relying on trans homophilic interactions between their extracellular cadherin (EC) repeat domains. We present the structure of the antiparallel EC1-4 homodimer of human PcdhγB3, a member of the γ subfamily of clustered Pcdhs. Structure and sequence comparisons of α, β, and γ clustered Pcdh isoforms illustrate that subfamilies encode specificity in distinct ways through diversification of loop region structure and composition in EC2 and EC3, which contains isoform-specific conservation of primarily polar residues. In contrast, the EC1/EC4 interface comprises hydrophobic interactions that provide non-selective dimerization affinity. Using sequence coevolution analysis, we found evidence for a similar antiparallel EC1-4 interaction in non-clustered Pcdh families. We thus deduce that the EC1-4 antiparallel homodimer is a general interaction strategy that evolved before the divergence of these distinct protocadherin families.

PubMed: 27472898
DOI: 10.7554/eLife.18449

実験手法

X-RAY DIFFRACTION (2.5 Å)