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3MW3

Crystal structure of beta-neurexin 2 with the splice insert 4

Summary for 3MW3
Entry DOI10.2210/pdb3mw3/pdb
Related3MW2 3MW4
DescriptorNeurexin-2-beta, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[beta-D-mannopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, CALCIUM ION, ... (4 entities in total)
Functional Keywordsneurexin, lns domain, calcium-binding, cell adhesion, glycoprotein
Biological sourceRattus norvegicus (rat)
Total number of polymer chains1
Total formula weight23565.34
Authors
Jin, X.,Shapiro, L. (deposition date: 2010-05-05, release date: 2010-07-28, Last modification date: 2024-11-06)
Primary citationKoehnke, J.,Katsamba, P.S.,Ahlsen, G.,Bahna, F.,Vendome, J.,Honig, B.,Shapiro, L.,Jin, X.
Splice Form Dependence of beta-Neurexin/Neuroligin Binding Interactions.
Neuron, 67:61-74, 2010
Cited by
PubMed Abstract: Alternatively spliced beta-neurexins (beta-NRXs) and neuroligins (NLs) are thought to have distinct extracellular binding affinities, potentially providing a beta-NRX/NL synaptic recognition code. We utilized surface plasmon resonance to measure binding affinities between all combinations of alternatively spliced beta-NRX 1-3 and NL 1-3 ectodomains. Binding was observed for all beta-NRX/NL pairs. The presence of the NL1 B splice insertion lowers beta-NRX binding affinity by approximately 2-fold, while beta-NRX splice insertion 4 has small effects that do not synergize with NL splicing. New structures of glycosylated beta-NRXs 1 and 2 containing splice insertion 4 reveal that the insertion forms a new beta strand that replaces the beta10 strand, leaving the NL binding site intact. This helps to explain the limited effect of splice insert 4 on NRX/NL binding affinities. These results provide new structural insights and quantitative binding information to help determine whether and how splice isoform choice plays a role in beta-NRX/NL-mediated synaptic recognition.
PubMed: 20624592
DOI: 10.1016/j.neuron.2010.06.001
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.33 Å)
Structure validation

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