2JLL
Crystal structure of NCAM2 IgIV-FN3II
Summary for 2JLL
| Entry DOI | 10.2210/pdb2jll/pdb |
| Related | 2DOC 2V5T 2VAJ 2WIM 2XY1 2XY2 2XYC |
| Descriptor | NEURAL CELL ADHESION MOLECULE 2, 2-acetamido-2-deoxy-beta-D-glucopyranose, GLYCEROL, ... (5 entities in total) |
| Functional Keywords | immunoglobulin domain, immunoglobulin superfamily, cell adhesion, transmembrane, phosphoprotein, neural, membrane, glycoprotein, cell membrane |
| 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 | 44713.06 |
| Authors | Kulahin, N.,Rasmussen, K.,Kristensen, O.,Kastrup, J.,Berezin, V.,Bock, E.,Walmod, P.,Gajhede, M. (deposition date: 2008-09-10, release date: 2009-11-17, Last modification date: 2020-07-29) |
| Primary citation | Kulahin, N.,Kristensen, O.,Rasmussen, K.K.,Olsen, L.,Rydberg, P.,Vestergaard, B.,Kastrup, J.S.,Berezin, V.,Bock, E.,Walmod, P.S.,Gajhede, M. Structural Model and Trans-Interaction of the Entire Ectodomain of the Olfactory Cell Adhesion Molecule. Structure, 19:203-, 2011 Cited by PubMed Abstract: The ectodomain of olfactory cell adhesion molecule (OCAM/NCAM2/RNCAM) consists of five immunoglobulin (Ig) domains (IgI-V), followed by two fibronectin-type 3 (Fn3) domains (Fn3I-II). A complete structural model of the entire ectodomain of human OCAM has been assembled from crystal structures of six recombinant proteins corresponding to different regions of the ectodomain. The model is the longest experimentally based composite structural model of an entire IgCAM ectodomain. It displays an essentially linear arrangement of IgI-V, followed by bends between IgV and Fn3I and between Fn3I and Fn3II. Proteins containing IgI-IgII domains formed stable homodimers in solution and in crystals. Dimerization could be disrupted in vitro by mutations in the dimer interface region. In conjunction with the bent ectodomain conformation, which can position IgI-V parallel with the cell surface, the IgI-IgII dimerization enables OCAM-mediated trans-interactions with an intercellular distance of about 20 nm, which is consistent with that observed in synapses. PubMed: 21300289DOI: 10.1016/J.STR.2010.12.014 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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