PDBsum entry 4ofp

Cell adhesion

PDB id: 4ofp

Contents

Protein chains

197 a.a.

Ligands

NAG ×6

PDB id:

4ofp

Name:

Cell adhesion

Title:

Crystal structure of syg-2 d3-d4

Structure:

Protein syg-2. Chain: a, b, c, d. Fragment: d3-d4, unp residues 231-430. Engineered: yes

Source:

Caenorhabditis elegans. Nematode. Organism_taxid: 6239. Gene: c26g2.1, cele_c26g2.1, syg-2. Expressed in: trichoplusia ni. Expression_system_taxid: 7111.

Resolution:

3.00Å R-factor: 0.244 R-free: 0.283

Authors:

E.Ozkan,K.C.Garcia

Key ref:

E.Özkan et al. (2014). Extracellular architecture of the SYG-1/SYG-2 adhesion complex instructs synaptogenesis. Cell, 156, 482-494. PubMed id: 24485456 DOI: 10.1016/j.cell.2014.01.004

Date:

15-Jan-14 Release date: 19-Feb-14

Protein chains

Q9U3P2  (SYG2_CAEEL) -  Synaptogenesis protein syg-2 from Caenorhabditis elegans

Seq: 1270 a.a.

Struc: 197 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

DOI no: 10.1016/j.cell.2014.01.004

Cell 156:482-494 (2014)

PubMed id: 24485456

Extracellular architecture of the SYG-1/SYG-2 adhesion complex instructs synaptogenesis.

E.Özkan, P.H.Chia, R.R.Wang, N.Goriatcheva, D.Borek, Z.Otwinowski, T.Walz, K.Shen, K.C.Garcia.

ABSTRACT

SYG-1 and SYG-2 are multipurpose cell adhesion molecules (CAMs) that have evolved across all major animal taxa to participate in diverse physiological functions, ranging from synapse formation to formation of the kidney filtration barrier. In the crystal structures of several SYG-1 and SYG-2 orthologs and their complexes, we find that SYG-1 orthologs homodimerize through a common, bispecific interface that similarly mediates an unusual orthogonal docking geometry in the heterophilic SYG-1/SYG-2 complex. C. elegans SYG-1's specification of proper synapse formation in vivo closely correlates with the heterophilic complex affinity, which appears to be tuned for optimal function. Furthermore, replacement of the interacting domains of SYG-1 and SYG-2 with those from CAM complexes that assume alternative docking geometries or the introduction of segmental flexibility compromised synaptic function. These results suggest that SYG extracellular complexes do not simply act as "molecular velcro" and that their distinct structural features are important in instructing synaptogenesis. PAPERFLICK: