5SZL
Protocadherin gamma A1 extracellular cadherin domains 1-4
Summary for 5SZL
Entry DOI | 10.2210/pdb5szl/pdb |
Related | 5SZM 5SZN 5SZO 5SZP 5SZQ 5SZR |
Descriptor | PROTOCADHERIN GAMMA A1 EXTRACELLULAR CADHERIN DOMAINS 1-4, Protein Pcdhga1, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total) |
Functional Keywords | cell adhesion |
Biological source | Mus musculus (Mouse) |
Total number of polymer chains | 4 |
Total formula weight | 195056.61 |
Authors | Goodman, K.M.,Bahna, F.,Mannepalli, S.,Honig, B.,Shapiro, L. (deposition date: 2016-08-14, release date: 2016-10-19, Last modification date: 2024-10-16) |
Primary citation | 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 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (4.2 Å) |
Structure validation
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