3MW3
Crystal structure of beta-neurexin 2 with the splice insert 4
Summary for 3MW3
| Entry DOI | 10.2210/pdb3mw3/pdb |
| Related | 3MW2 3MW4 |
| Descriptor | Neurexin-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 Keywords | neurexin, lns domain, calcium-binding, cell adhesion, glycoprotein |
| Biological source | Rattus norvegicus (rat) |
| Total number of polymer chains | 1 |
| Total formula weight | 23565.34 |
| Authors | Jin, X.,Shapiro, L. (deposition date: 2010-05-05, release date: 2010-07-28, Last modification date: 2024-11-06) |
| Primary citation | Koehnke, 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: 20624592DOI: 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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