5KC7: Crystal Structure Of Cbln1 (val55-gly58 Deletion Mutant)

Ionotropic glutamate receptor (iGluR) family members are integrated into supramolecular complexes that modulate their location and function at excitatory synapses. However, a lack of structural information beyond isolated receptors or fragments thereof currently limits the mechanistic understanding of physiological iGluR signaling. Here, we report structural and functional analyses of the prototypical molecular bridge linking postsynaptic iGluR delta2 (GluD2) and presynaptic beta-neurexin 1 (beta-NRX1) via Cbln1, a C1q-like synaptic organizer. We show how Cbln1 hexamers "anchor" GluD2 amino-terminal domain dimers to monomeric beta-NRX1. This arrangement promotes synaptogenesis and is essential for D: -serine-dependent GluD2 signaling in vivo, which underlies long-term depression of cerebellar parallel fiber-Purkinje cell (PF-PC) synapses and motor coordination in developing mice. These results lead to a model where protein and small-molecule ligands synergistically control synaptic iGluR function.
PDB ID: 5KC7Download
MMDB ID: 141404
PDB Deposition Date: 2016/6/5
Updated in MMDB: 2016/08
Experimental Method:
x-ray diffraction
Resolution: 7.04  Å
Source Organism:
Similar Structures:
Biological Unit for 5KC7: hexameric; determined by author
Molecular Components in 5KC7
Label Count Molecule
Proteins (6 molecules)
Cerebellin-1(Gene symbol: CBLN1)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB