Crystal Structures of Beta-Neurexin 1 and Beta-Neurexin 2 Ectodomains and Dynamics of Splice Insertion Sequence 4
Presynaptic neurexins (NRXs) bind to postsynaptic neuroligins (NLs) to form Ca{sup 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{sup 2+} ions. The Ca{sup 2+}-binding site is disordered in the {beta}-NRX2 structure, but the 1.7 {angstrom} {beta}-NRX1 structure reveals a single Ca{sup 2+} ion, {approx}12 {angstrom} 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.
- Research Organization:
- Brookhaven National Laboratory (BNL) National Synchrotron Light Source
- Sponsoring Organization:
- Doe - Office Of Science
- DOE Contract Number:
- AC02-98CH10886
- OSTI ID:
- 980111
- Report Number(s):
- BNL--93029-2010-JA
- Journal Information:
- Structure, Journal Name: Structure Journal Issue: 3 Vol. 16
- Country of Publication:
- United States
- Language:
- English
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