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Structure paper

TitleStructural basis for variant-specific neuroligin-binding by α-neurexin.
Journal, issue, pagesPLoS One, Vol. 6, Issue 4, Page e19411, Year 2011
Publish dateApr 28, 2011
AuthorsHiroki Tanaka / Terukazu Nogi / Norihisa Yasui / Kenji Iwasaki / Junichi Takagi /
PubMed AbstractNeurexins (Nrxs) are presynaptic membrane proteins with a single membrane-spanning domain that mediate asymmetric trans-synaptic cell adhesion by binding to their postsynaptic receptor neuroligins. ...Neurexins (Nrxs) are presynaptic membrane proteins with a single membrane-spanning domain that mediate asymmetric trans-synaptic cell adhesion by binding to their postsynaptic receptor neuroligins. α-Nrx has a large extracellular region comprised of multiple copies of laminin, neurexin, sex-hormone-binding globulin (LNS) domains and epidermal growth factor (EGF) modules, while that of β-Nrx has but a single LNS domain. It has long been known that the larger α-Nrx and the shorter β-Nrx show distinct binding behaviors toward different isoforms/variants of neuroligins, although the underlying mechanism has yet to be elucidated. Here, we describe the crystal structure of a fragment corresponding to the C-terminal one-third of the Nrx1α ectodomain, consisting of LNS5-EGF3-LNS6. The 2.3 Å-resolution structure revealed the presence of a domain configuration that was rigidified by inter-domain contacts, as opposed to the more common flexible "beads-on-a-string" arrangement. Although the neuroligin-binding site on the LNS6 domain was completely exposed, the location of the α-Nrx specific LNS5-EGF3 segment proved incompatible with the loop segment inserted in the B+ neuroligin variant, which explains the variant-specific neuroligin recognition capability observed in α-Nrx. This, combined with a low-resolution molecular envelope obtained by a single particle reconstruction performed on negatively stained full-length Nrx1α sample, allowed us to derive a structural model of the α-Nrx ectodomain. This model will help us understand not only how the large α-Nrx ectodomain is accommodated in the synaptic cleft, but also how the trans-synaptic adhesion mediated by α- and β-Nrxs could differentially affect synaptic structure and function.
External linksPLoS One / PubMed:21552542 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution2.3 Å
Structure data

EMDB-5270:
The entire ectodomain of bovine Nrx1alpha
Method: EM (single particle)

PDB-3asi:
Alpha-Neurexin-1 ectodomain fragment; LNS5-EGF3-LNS6
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-HOH:
WATER

Source
  • unidentified (others)
  • bos taurus (cattle)
KeywordsCELL ADHESION / Beta-sandwich / synapse maturation / Neuroligin / N-glycosylation / Membrane

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