3VKF

Crystal Structure of Neurexin 1beta/Neuroligin 1 complex

Summary for 3VKF

• Entry DOI: 10.2210/pdb3vkf/pdb
• Descriptor: Neuroligin-1, Neurexin-1-beta, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• Functional Keywords: alpha/beta hydrolase, beta-sandwich, synapse matulation, calcium binding, n-glycosylation, membrane, cell adhesion
• Biological source: Rattus norvegicus (rat); More
• Total number of polymer chains: 4
• Total formula weight: 170934.05

Authors

Tanaka, H.,Miyazaki, N.,Nogi, T.,Iwasaki, K.,Takagi, J. (deposition date: 2011-11-15, release date: 2012-08-01, Last modification date: 2024-11-06)

Primary citation

Tanaka, H.,Miyazaki, N.,Matoba, K.,Nogi, T.,Iwasaki, K.,Takagi, J.
Higher-order architecture of cell adhesion mediated by polymorphic synaptic adhesion molecules neurexin and neuroligin.
Cell Rep, 2:101-110, 2012

PubMed Abstract: Polymorphic adhesion molecules neurexin and neuroligin (NL) mediate asymmetric trans-synaptic adhesion, which is crucial for synapse development and function. It is not known whether or how individual synapse function is controlled by the interactions between variants and isoforms of these molecules with differing ectodomain regions. At a physiological concentration of Ca(2+), the ectodomain complex of neurexin-1 β isoform (Nrx1β) and NL1 spontaneously assembled into crystals of a lateral sheet-like superstructure topologically compatible with transcellular adhesion. Correlative light-electron microscopy confirmed extracellular sheet formation at the junctions between Nrx1β- and NL1-expressing non-neuronal cells, mimicking the close, parallel synaptic membrane apposition. The same NL1-expressing cells, however, did not form this higher-order architecture with cells expressing the much longer neurexin-1 α isoform, suggesting a functional discrimination mechanism between synaptic contacts made by different isoforms of neurexin variants.

PubMed: 22840401
DOI: 10.1016/j.celrep.2012.06.009

Experimental method

X-RAY DIFFRACTION (3.3 Å)