PDBsum entry: 1qz1

Cell adhesion

PDB id: 1qz1

Contents

Protein chain

288 a.a. *

Waters ×265

* Residue conservation analysis

PDB id:

1qz1

Name:

Cell adhesion

Title:

Crystal structure of the ig 1-2-3 fragment of ncam

Structure:

Neural cell adhesion molecule 1, 140 kda isoform. Chain: a. Fragment: ig modules 1-2-3. Synonym: n-cam 140, ncam-140. Engineered: yes

Source:

Rattus norvegicus. Norway rat. Organism_taxid: 10116. Gene: ncam1. Expressed in: pichia pastoris. Expression_system_taxid: 4922.

Resolution:

2.00Å R-factor: 0.218 R-free: 0.238

Authors:

V.Soroka,K.Kolkova,J.S.Kastrup,K.Diederichs,J.Breed, V.V.Kiselyov,F.M.Poulsen,I.K.Larsen,W.Welte,V.Berezin, E.Bock,C.Kasper

Key ref:

V.Soroka et al. (2003). Structure and interactions of NCAM Ig1-2-3 suggest a novel zipper mechanism for homophilic adhesion. Structure, 11, 1291-1301. PubMed id: 14527396 DOI: 10.1016/j.str.2003.09.006

Date:

15-Sep-03 Release date: 04-Nov-03

Protein chain

P13596  (NCAM1_RAT) -  Neural cell adhesion molecule 1

Seq: 858 a.a.

Struc: 288 a.a.*

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

 Gene Ontology (GO) functional annotation 

• Cellular component: membrane (1 term)
• Biological process: cell adhesion (1 term)

DOI no: 10.1016/j.str.2003.09.006

Structure 11:1291-1301 (2003)

PubMed id: 14527396

Structure and interactions of NCAM Ig1-2-3 suggest a novel zipper mechanism for homophilic adhesion.

V.Soroka, K.Kolkova, J.S.Kastrup, K.Diederichs, J.Breed, V.V.Kiselyov, F.M.Poulsen, I.K.Larsen, W.Welte, V.Berezin, E.Bock, C.Kasper.

ABSTRACT

The neural cell adhesion molecule, NCAM, mediates Ca(2+)-independent cell-cell and cell-substratum adhesion via homophilic (NCAM-NCAM) and heterophilic (NCAM-non-NCAM molecules) binding. NCAM plays a key role in neural development, regeneration, and synaptic plasticity, including learning and memory consolidation. The crystal structure of a fragment comprising the three N-terminal Ig modules of rat NCAM has been determined to 2.0 A resolution. Based on crystallographic data and biological experiments we present a novel model for NCAM homophilic binding. The Ig1 and Ig2 modules mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), whereas the Ig3 module mediates interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through simultaneous binding to the Ig1 and Ig2 modules. This arrangement results in two perpendicular zippers forming a double zipper-like NCAM adhesion complex.

Selected figure(s)

Figure 3.
Figure 3. Closeup View of the Interaction Interfaces in the NCAM Ig1-2-3 Fragment(A) The Ig1-to-Ig2 interaction interface. The Ig1 and Ig2 modules are shown in yellow and green and belong to two different Ig1-2-3 fragments that form one Ig1-2-3 cis dimer.(B) The Ig2-to-Ig3 interaction interface.(C) The Ig2-to-Ig2 interaction interface.(D) The Ig1-to-Ig3 interaction interface.In (B)-(D), the ribbon representations of modules from two interacting Ig1-2-3 fragments belonging to different Ig1-2-3 cis dimers are shown in green and cyan. Oxygen atoms are shown in red and nitrogens in blue. The hydrogen bonds are shown as red dashed lines. Water molecules are shown as red spheres.

The above figure is reprinted by permission from Cell Press: Structure (2003, 11, 1291-1301) copyright 2003.

Figure was selected by an automated process.