5L2E

Crystal structure of rat Glutamate receptor delta-2 extracellular domain

Summary for 5L2E

• Entry DOI: 10.2210/pdb5l2e/pdb
• Descriptor: Glutamate receptor ionotropic, delta-2,Glutamate receptor ionotropic, delta-2 (1 entity in total)
• Functional Keywords: synapse protein, cell surface protein, glycoprotein, nervous system, protein binding
• Biological source: Rattus norvegicus (Rat); More
• Cellular location: Cell membrane ; Multi-pass membrane protein : Q63226
• Total number of polymer chains: 3
• Total formula weight: 233501.44

Authors

Cheng, S.,Ozkan, E. (deposition date: 2016-08-01, release date: 2016-12-28, Last modification date: 2024-10-23)

Primary citation

Cheng, S.,Seven, A.B.,Wang, J.,Skiniotis, G.,Ozkan, E.
Conformational Plasticity in the Transsynaptic Neurexin-Cerebellin-Glutamate Receptor Adhesion Complex.
Structure, 24:2163-2173, 2016

PubMed Abstract: Synaptic specificity is a defining property of neural networks. In the cerebellum, synapses between parallel fiber neurons and Purkinje cells are specified by the simultaneous interactions of secreted protein cerebellin with pre-synaptic neurexin and post-synaptic delta-type glutamate receptors (GluD). Here, we determined the crystal structures of the trimeric C1q-like domain of rat cerebellin-1, and the first complete ectodomain of a GluD, rat GluD2. Cerebellin binds to the LNS6 domain of α- and β-neurexin-1 through a high-affinity interaction that involves its highly flexible N-terminal domain. In contrast, we show that the interaction of cerebellin with isolated GluD2 ectodomain is low affinity, which is not simply an outcome of lost avidity when compared with binding with a tetrameric full-length receptor. Rather, high-affinity capture of cerebellin by post-synaptic terminals is likely controlled by long-distance regulation within this transsynaptic complex. Altogether, our results suggest unusual conformational flexibility within all components of the complex.

PubMed: 27926833
DOI: 10.1016/j.str.2016.11.004

Experimental method

X-RAY DIFFRACTION (4.152 Å)