3BOD
Structure of mouse beta-neurexin 1
Summary for 3BOD
| Entry DOI | 10.2210/pdb3bod/pdb |
| Descriptor | Neurexin-1-alpha, CALCIUM ION (3 entities in total) |
| Functional Keywords | neurexin1d, lns6, alternative splicing, calcium, cell adhesion, egf-like domain, glycoprotein, membrane, metal-binding, transmembrane |
| Biological source | Mus musculus (house mouse) More |
| Cellular location | Cell membrane ; Single-pass type I membrane protein : Q9CS84 |
| Total number of polymer chains | 1 |
| Total formula weight | 19351.79 |
| Authors | Koehnke, J.,Jin, X.,Shapiro, L. (deposition date: 2007-12-17, release date: 2008-03-25, Last modification date: 2024-02-21) |
| Primary citation | Koehnke, J.,Jin, X.,Trbovic, N.,Katsamba, P.S.,Brasch, J.,Ahlsen, G.,Scheiffele, P.,Honig, B.,Palmer, A.G.,Shapiro, L. Crystal Structures of beta-Neurexin 1 and beta-Neurexin 2 Ectodomains and Dynamics of Splice Insertion Sequence 4. Structure, 16:410-421, 2008 Cited by PubMed Abstract: Presynaptic neurexins (NRXs) bind to postsynaptic neuroligins (NLs) to form Ca(2+)-dependent complexes that bridge neural synapses. beta-NRXs bind NLs through their LNS domains, which contain a single site of alternative splicing (splice site 4) giving rise to two isoforms: +4 and Delta. We present crystal structures of the Delta isoforms of the LNS domains from beta-NRX1 and beta-NRX2, crystallized in the presence of Ca(2+) ions. The Ca(2+)-binding site is disordered in the beta-NRX2 structure, but the 1.7 A beta-NRX1 structure reveals a single Ca(2+) ion, approximately 12 A from the splice insertion site, with one coordinating ligand donated by a glutamic acid from an adjacent beta-NRX1 molecule. NMR studies of beta-NRX1+4 show that the insertion sequence is unstructured, and remains at least partially disordered in complex with NL. These results raise the possibility that beta-NRX insertion sequence 4 may function in roles independent of neuroligin binding. PubMed: 18334216DOI: 10.1016/j.str.2007.12.024 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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