2H0B
Crystal Structure of the second LNS/LG domain from Neurexin 1 alpha
Summary for 2H0B
| Entry DOI | 10.2210/pdb2h0b/pdb |
| Descriptor | Neurexin-1-alpha, CALCIUM ION, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | b-sandwich, cell adhesion |
| Biological source | Bos taurus (cattle) |
| Cellular location | Cell membrane ; Single-pass type I membrane protein : Q28146 |
| Total number of polymer chains | 4 |
| Total formula weight | 81941.37 |
| Authors | Sheckler, L.R.,Henry, L.,Sugita, S.,Sudhof, T.C.,Rudenko, G. (deposition date: 2006-05-14, release date: 2006-06-20, Last modification date: 2024-11-20) |
| Primary citation | Sheckler, L.R.,Henry, L.,Sugita, S.,Sudhof, T.C.,Rudenko, G. Crystal Structure of the Second LNS/LG Domain from Neurexin 1{alpha}: Ca2+ binding and the effects of alternative splicing J.Biol.Chem., 281:22896-22905, 2006 Cited by PubMed Abstract: Neurexins mediate protein interactions at the synapse, playing an essential role in synaptic function. Extracellular domains of neurexins, and their fragments, bind a distinct profile of different proteins regulated by alternative splicing and Ca2+. The crystal structure of n1alpha_LNS#2 (the second LNS/LG domain of bovine neurexin 1alpha) reveals large structural differences compared with n1alpha_LNS#6 (or n1beta_LNS), the only other LNS/LG domain for which a structure has been determined. The differences overlap the so-called hyper-variable surface, the putative protein interaction surface that is reshaped as a result of alternative splicing. A Ca2+-binding site is revealed at the center of the hyper-variable surface next to splice insertion sites. Isothermal titration calorimetry indicates that the Ca2+-binding site in n1alpha_LNS#2 has low affinity (Kd approximately 400 microm). Ca2+ binding ceases to be measurable when an 8- or 15-residue splice insert is present at the splice site SS#2 indicating that alternative splicing can affect Ca2+-binding sites of neurexin LNS/LG domains. Our studies initiate a framework for the putative protein interaction sites of neurexin LNS/LG domains. This framework is essential to understand how incorporation of alternative splice inserts expands the information from a limited set of neurexin genes to produce a large array of synaptic adhesion molecules with potentially very different synaptic function. PubMed: 16772286DOI: 10.1074/jbc.M603464200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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