2VAJ

Crystal structure of NCAM2 Ig1 (I4122 cell unit)

Summary for 2VAJ

• Entry DOI: 10.2210/pdb2vaj/pdb
• Related: 2DOC 2V44 2V5T 2VA4
• Descriptor: NEURAL CELL ADHESION MOLECULE 2 (2 entities in total)
• Functional Keywords: immunoglobulin domain, cell adhesion
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Cell membrane; Single-pass type I membrane protein: O15394
• Total number of polymer chains: 1
• Total formula weight: 10364.62

Authors

Kulahin, N.,Rasmussen, K.K.,Kristensen, O.,Kastrup, J.S.,Navarro-Poulsen, J.-C.,Berezin, V.,Bock, E.,Walmod, P.S.,Gajhede, M. (deposition date: 2007-08-31, release date: 2008-08-26, Last modification date: 2024-10-23)

Primary citation

Rasmussen, K.K.,Kulahin, N.,Kristensen, O.,Poulsen, J.C.,Sigurskjold, B.W.,Kastrup, J.S.,Berezin, V.,Bock, E.,Walmod, P.S.,Gajhede, M.
Crystal Structure of the Ig1 Domain of the Neural Cell Adhesion Molecule Ncam2 Displays Domain Swapping.
J.Mol.Biol., 382:1113-, 2008

PubMed Abstract: The crystal structure of the first immunoglobulin (Ig1) domain of neural cell adhesion molecule 2 (NCAM2/OCAM/RNCAM) is presented at a resolution of 2.7 A. NCAM2 is a member of the immunoglobulin superfamily of cell adhesion molecules (IgCAMs). In the structure, two Ig domains interact by domain swapping, as the two N-terminal beta-strands are interchanged. beta-Strand swapping at the terminal domain is the accepted mechanism of homophilic interactions amongst the cadherins, another class of CAMs, but it has not been observed within the IgCAM superfamily. Gel-filtration chromatography demonstrated the ability of NCAM2 Ig1 to form dimers in solution. Taken together, these observations suggest that beta-strand swapping could have a role in the molecular mechanism of homophilic binding for NCAM2.

PubMed: 18706912
DOI: 10.1016/J.JMB.2008.07.084

Experimental method

X-RAY DIFFRACTION (2.701 Å)