2xy1

CRYSTAL STRUCTURE OF NCAM2 IG3-4

spinqualitylabelsall models 2xy1, resolution 1.98Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2xy1 is a 1 chain structure with sequence from Homo sapiens. This structure supersedes the now removed PDB entry 2va4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.979Å Ligands: NAG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function NCAM2_HUMAN May play important roles in selective fasciculation and zone-to-zone projection of the primary olfactory axons. Publication Abstract from PubMed 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. Structural Model and trans-Interaction of the Entire Ectodomain of the Olfactory Cell Adhesion Molecule.,Kulahin N, Kristensen O, Rasmussen KK, Olsen L, Rydberg P, Vestergaard B, Kastrup JS, Berezin V, Bock E, Walmod PS, Gajhede M Structure. 2011 Feb 9;19(2):203-11. PMID:21300289 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA