PDBsum entry 4zi9

Cell adhesion

PDB id: 4zi9

Contents

Protein chains

309 a.a.

Metals

_CA ×12

Waters ×477

PDB id:

4zi9

Name:

Cell adhesion

Title:

Structure of mouse clustered pcdhga1 ec1-3

Structure:

Mcg133388, isoform cra_t. Chain: a, b. Fragment: unp residues 29-339. Synonym: protein pcdhga1,protocadherin gamma a1. Engineered: yes

Source:

Mus musculus. Mouse. Organism_taxid: 10090. Gene: pcdhga1, mcg_133388. Expressed in: escherichia coli. Expression_system_taxid: 511693.

Resolution:

1.70Å R-factor: 0.231 R-free: 0.266

Authors:

J.M.Nicoludis,S.-Y.Lau,C.P.I.Scharfe,D.S.Marks,W.A.Weihofen,R.Gaudet

Key ref:

J.M.Nicoludis et al. (2015). Structure and Sequence Analyses of Clustered Protocadherins Reveal Antiparallel Interactions that Mediate Homophilic Specificity. Structure, 23, 2087-2098. PubMed id: 26481813 DOI: 10.1016/j.str.2015.09.005

Date:

27-Apr-15 Release date: 28-Oct-15

Protein chains

Q91XZ0  (Q91XZ0_MOUSE) -  Protocadherin gamma A1 from Mus musculus

Seq: 931 a.a.

Struc: 309 a.a.

DOI no: 10.1016/j.str.2015.09.005

Structure 23:2087-2098 (2015)

PubMed id: 26481813

Structure and Sequence Analyses of Clustered Protocadherins Reveal Antiparallel Interactions that Mediate Homophilic Specificity.

J.M.Nicoludis, S.Y.Lau, C.P.Schärfe, D.S.Marks, W.A.Weihofen, R.Gaudet.

ABSTRACT

Clustered protocadherin (Pcdh) proteins mediate dendritic self-avoidance in neurons via specific homophilic interactions in their extracellular cadherin (EC) domains. We determined crystal structures of EC1-EC3, containing the homophilic specificity-determining region, of two mouse clustered Pcdh isoforms (PcdhγA1 and PcdhγC3) to investigate the nature of the homophilic interaction. Within the crystal lattices, we observe antiparallel interfaces consistent with a role in trans cell-cell contact. Antiparallel dimerization is supported by evolutionary correlations. Two interfaces, located primarily on EC2-EC3, involve distinctive clustered Pcdh structure and sequence motifs, lack predicted glycosylation sites, and contain residues highly conserved in orthologs but not paralogs, pointing toward their biological significance as homophilic interaction interfaces. These two interfaces are similar yet distinct, reflecting a possible difference in interaction architecture between clustered Pcdh subfamilies. These structures initiate a molecular understanding of clustered Pcdh assemblies that are required to produce functional neuronal networks.