5SZQ
Protocadherin Gamma A4 extracellular cadherin domains 3-6
Summary for 5SZQ
| Entry DOI | 10.2210/pdb5szq/pdb |
| Related | 5SZL 5SZM 5SZN 5SZO 5SZP 5SZR |
| Descriptor | Protocadherin gamma-A4, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose, ... (5 entities in total) |
| Functional Keywords | cell adhesion |
| Biological source | Mus musculus (Mouse) |
| Cellular location | Cell membrane ; Single-pass type I membrane protein : Q91XY4 |
| Total number of polymer chains | 1 |
| Total formula weight | 50148.00 |
| Authors | Goodman, K.M.,Mannepalli, S.,Bahna, F.,Honig, B.,Shapiro, L. (deposition date: 2016-08-14, release date: 2016-11-02, Last modification date: 2024-10-09) |
| 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 (2.608 Å) |
Structure validation
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