1EPF


Conserved Protein Domain Family
IgI_1_NCAM-1

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cd05865: IgI_1_NCAM-1 
Click on image for an interactive view with Cn3D
First immunoglobulin (Ig)-like domain of neural cell adhesion molecule (NCAM-1); member of the I-set of Ig superfamily (IgSF) domains
The members here are composed of the first immunoglobulin (Ig)-like domain of neural cell adhesion molecule (NCAM-1). NCAM-1 plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-nonNCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves the Ig1, Ig2, and Ig3 domains. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.
Statistics
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PSSM-Id: 409451
View PSSM: cd05865
Aligned: 4 rows
Threshold Bit Score: 184.088
Threshold Setting Gi: 127855
Created: 11-Jan-2008
Updated: 17-Aug-2020
Structure
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Program:
Drawing:
Aligned Rows:
  next features
Conserved site includes 3 residues -Click on image for an interactive view with Cn3D
Feature 1:dimer interface [polypeptide binding site]
Evidence:
  • Structure:1EPF, rat neural cell adhesion molecule (NCAM) dimer showing Ig1-Ig2 dimer interface, contacts based on 3.5 A distance.
    View structure with Cn3D
  • Comment:Dimerization mediates cell-cell recognition and adhesion.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                     # ##                                                             
1EPF_A       3 LQVDIVPSQGEISVGESKFFLCQVAGdakdKDISWFSPNGEKLsPNQQRISVVWNDDDSSTLTIYNANIDDAGIYKCVVT 82   Norway rat
127855      20 LEVNIVPDQGEISLGESKFFLCQVSGe--aTDISWYSPTGEKL-VTQQQISVVRSDDYTSTLTIYNASSQDAGIYKCVAS 96   African clawed frog
P13590      20 LQVDIVPSQGEISVGESKFFLCQVAGeakyKDISWFSPNGEKLtPNQQRISVVRNDDFSSTLTIYNANIDDAGIYKCVVS 99   chicken
EAW67201    20 LQVDIVPSQGEISVGESKFFLCQVAGdakdKDISWFSPNGEKLtPNQQRISVVWNDDSSSTLTIYNANIDDAGIYKCVVT 99   human
Feature 1                       
1EPF_A      83 AEDGTQSEATVNVKIFQ 99   Norway rat
127855      97 NEAEGESEGTVNLKIYQ 113  African clawed frog
P13590     100 SVEEGDSEATVNVKIFQ 116  chicken
EAW67201   100 GEDGSESEATVNVKIFQ 116  human

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