7mrn | pdb_00007mrn

Mouse CNTN5 APP complex

spinqualitylabelsall models 7mrn, resolution 3.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7mrn is a 4 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.5Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CNTN5_MOUSE Contactins mediate cell surface interactions during nervous system development. Has some neurite outgrowth-promoting activity in the cerebral cortical neurons but not in hippocampal neurons (By similarity). Involved in neuronal activity in the auditory system. Publication Abstract from PubMed Contactins (CNTN) are neural cell adhesion molecules that encode axon-target specificity during the patterning of the vertebrate visual and olfactory systems. Because CNTNs are tethered to the plasma membrane by a glycosylphosphatidylinositol anchor, they lack an intracellular region to communicate across the membrane. Instead, they form co-receptor complexes with distinct transmembrane proteins to transmit signals inside the cell. In particular, a complex of CNTN4 and amyloid precursor protein (APP) is known to guide the assembly of specific circuits in the visual system. Here, using in situ hybridization in zebrafish embryos, we show that CNTN4, CNTN5, and the APP homologues APLP1 and APLP2 are expressed in olfactory pits, suggesting that these receptors may also function together in the organization of olfactory tissues. Furthermore, we use biochemical and structural approaches to characterize interactions between members of these two receptor families. In particular, APP and APLP1 interact with CNTN3-5, while APLP2 only binds to CNTN4 and 5. Finally, structural analyses of five CNTN/amyloid pairs indicate that these proteins interact through a conserved interface involving the second fibronectin type III repeat of CNTNs and the copper-binding domain of amyloid proteins. Overall, this work sets the stage for analyzing CNTN/amyloid-mediated connectivity in vertebrate sensory circuits. Members of the vertebrate contactin and amyloid precursor protein families interact through a conserved interface.,Karuppan SJ, Vogt A, Fischer Z, Ladutska A, Swiastyn J, McGraw HF, Bouyain S J Biol Chem. 2021 Dec 24:101541. doi: 10.1016/j.jbc.2021.101541. PMID:34958801 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA