5SZP

Protocadherin Gamma B7 extracellular cadherin domains 1-4 P21 crystal form

Summary for 5SZP

• Entry DOI: 10.2210/pdb5szp/pdb
• Related: 5SZL 5SZM 5SZN 5SZO 5SZQ
• Descriptor: Protocadherin Gamma B7, CALCIUM ION, alpha-D-mannopyranose, ... (6 entities in total)
• Functional Keywords: cell adhesion
• Biological source: Mus musculus (Mouse)
• Cellular location: Cell membrane ; Single-pass type I membrane protein : Q91XX3
• Total number of polymer chains: 2
• Total formula weight: 96869.91

Authors

Goodman, K.M.,Mannepalli, S.,Bahna, F.,Honig, B.,Shapiro, L. (deposition date: 2016-08-14, release date: 2016-10-19, Last modification date: 2024-10-30)

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

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: 27782885
DOI: 10.7554/eLife.20930

Experimental method

X-RAY DIFFRACTION (3.1 Å)