5T9T
Protocadherin Gamma B2 extracellular cadherin domains 1-5
5T9T の概要
エントリーDOI | 10.2210/pdb5t9t/pdb |
分子名称 | Protocadherin gamma B2-alpha C, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, CALCIUM ION, ... (6 entities in total) |
機能のキーワード | 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 : Q8K486 |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 123261.47 |
構造登録者 | Goodman, K.M.,Mannepalli, S.,Bahna, F.,Honig, B.,Shapiro, L. (登録日: 2016-09-09, 公開日: 2016-10-19, 最終更新日: 2023-10-04) |
主引用文献 | Goodman, K.M.,Rubinstein, R.,Thu, C.A.,Mannepalli, S.,Bahna, F.,Ahlsen, G.,Rittenhouse, C.,Maniatis, T.,Honig, B.,Shapiro, L. gamma-Protocadherin structural diversity and functional implications. Elife, 5:-, 2016 Cited by PubMed Abstract: Stochastic cell-surface expression of α-, β-, and γ-clustered protocadherins (Pcdhs) provides vertebrate neurons with single-cell identities that underlie neuronal self-recognition. Here we report crystal structures of ectodomain fragments comprising cell-cell recognition regions of mouse γ-Pcdhs γA1, γA8, γB2, and γB7 revealing -homodimers, and of C-terminal ectodomain fragments from γ-Pcdhs γA4 and γB2, which depict -interacting regions in monomeric form. Together these structures span the entire γ-Pcdh ectodomain. The -dimer structures reveal determinants of γ-Pcdh isoform-specific homophilic recognition. We identified and structurally mapped -dimerization mutations to the C-terminal ectodomain structures. Biophysical studies showed that Pcdh ectodomains from γB-subfamily isoforms formed dimers, whereas γA isoforms did not, but both γA and γB isoforms could interact in with α-Pcdhs. Together, these data show how interaction specificity is distributed over all domains of the γ-Pcdh interface, and suggest that subfamily- or isoform-specific -interactions may play a role in the Pcdh-mediated neuronal self-recognition code. PubMed: 27782885DOI: 10.7554/eLife.20930 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (3.5 Å) |
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