PDBsum entry 5dzx

Cell adhesion

PDB id: 5dzx

Contents

Protein chains

414 a.a.

Ligands

NAG-NAG-BMA-MAN-FUC ×2

NAG-NAG

MAN ×3

Metals

_CA ×18

Waters ×7

PDB id:

5dzx

Name:

Cell adhesion

Title:

Protocadherin beta 6 extracellular cadherin domains 1-4

Structure:

Protocadherin beta 6. Chain: a, b. Fragment: unp residues 29-445. Engineered: yes

Source:

Mus musculus. Mouse. Organism_taxid: 10090. Gene: pcdhb6. Expressed in: homo sapiens. Expression_system_taxid: 9606. Expression_system_cell_line: hek293f

Resolution:

2.88Å R-factor: 0.244 R-free: 0.289

Authors:

K.M.Goodman,S.Mannepalli,F.Bahna,B.Honig,L.Shapiro

Key ref:

K.M.Goodman et al. (2016). Structural Basis of Diverse Homophilic Recognition by Clustered α- and β-Protocadherins. Neuron, 90, 709-723. PubMed id: 27161523 DOI: 10.1016/j.neuron.2016.04.004

Date:

26-Sep-15 Release date: 04-May-16

Protein chains

Q91XZ4  (PCDB6_MOUSE) -  Protocadherin beta-6 from Mus musculus

Seq: 772 a.a.

Struc: 414 a.a.

DOI no: 10.1016/j.neuron.2016.04.004

Neuron 90:709-723 (2016)

PubMed id: 27161523

Structural Basis of Diverse Homophilic Recognition by Clustered α- and β-Protocadherins.

K.M.Goodman, R.Rubinstein, C.A.Thu, F.Bahna, S.Mannepalli, G.Ahlsén, C.Rittenhouse, T.Maniatis, B.Honig, L.Shapiro.

ABSTRACT

Clustered protocadherin proteins (α-, β-, and γ-Pcdhs) provide a high level of cell-surface diversity to individual vertebrate neurons, engaging in highly specific homophilic interactions to mediate important roles in mammalian neural circuit development. How Pcdhs bind homophilically through their extracellular cadherin (EC) domains among dozens of highly similar isoforms has not been determined. Here, we report crystal structures for extracellular regions from four mouse Pcdh isoforms (α4, α7, β6, and β8), revealing a canonical head-to-tail interaction mode for homophilic trans dimers comprising primary intermolecular EC1:EC4 and EC2:EC3 interactions. A subset of trans interface residues exhibit isoform-specific conservation, suggesting roles in recognition specificity. Mutation of these residues, along with trans-interacting partner residues, altered the specificities of Pcdh interactions. Together, these data show how sequence variation among Pcdh isoforms encodes their diverse strict homophilic recognition specificities, which are required for their key roles in neural circuit assembly.