3biw: Difference between revisions
New page: left|200px<br /><applet load="3biw" size="450" color="white" frame="true" align="right" spinBox="true" caption="3biw, resolution 3.500Å" /> '''Crystal structure o... |
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'''Crystal structure of the Neuroligin-1/Neurexin-1beta synaptic adhesion complex'''<br /> | '''Crystal structure of the Neuroligin-1/Neurexin-1beta synaptic adhesion complex'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
3BIW is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=NAG: | 3BIW is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=NAG:'>NAG</scene> and <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BIW OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: transmembrane]] | [[Category: transmembrane]] | ||
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Revision as of 09:14, 23 January 2008
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Crystal structure of the Neuroligin-1/Neurexin-1beta synaptic adhesion complex
Overview
Neurexins and neuroligins provide trans-synaptic connectivity by the, Ca(2+)-dependent interaction of their alternatively spliced extracellular, domains. Neuroligins specify synapses in an activity-dependent manner, presumably by binding to neurexins. Here, we present the crystal, structures of neuroligin-1 in isolation and in complex with, neurexin-1beta. Neuroligin-1 forms a constitutive dimer, and two, neurexin-1beta monomers bind to two identical surfaces on the opposite, faces of the neuroligin-1 dimer to form a heterotetramer. The, neuroligin-1/neurexin-1beta complex exhibits a nanomolar affinity and, includes a large binding interface that contains bound Ca(2+)., Alternatively spliced sites in neurexin-1beta and in neuroligin-1 are, positioned nearby the binding interface, explaining how they regulate the, interaction. Structure-based mutations of neuroligin-1 at the interface, disrupt binding to neurexin-1beta, but not the folding of neuroligin-1 and, confirm the validity of the binding interface of the, neuroligin-1/neurexin-1beta complex. Our results provide molecular, insights for understanding the role of cell-adhesion proteins in synapse, function.
About this Structure
3BIW is a Protein complex structure of sequences from Rattus norvegicus with NAG and CA as ligands. Full crystallographic information is available from OCA.
Reference
Structures of Neuroligin-1 and the Neuroligin-1/Neurexin-1beta Complex Reveal Specific Protein-Protein and Protein-Ca(2+) Interactions., Arac D, Boucard AA, Ozkan E, Strop P, Newell E, Sudhof TC, Brunger AT, Neuron. 2007 Dec 20;56(6):992-1003. PMID:18093522
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Proteopedia Page Contributors and Editors (what is this?)
- Pages with broken file links
- Protein complex
- Rattus norvegicus
- Arac, D.
- Boucard, A.A.
- Brunger, A.T.
- Newell, E.
- Ozkan, E.
- Strop, P.
- Sudhof, T.C.
- CA
- NAG
- Alpha-beta hydrolase
- Alternative promoter usage
- Alternative splicing
- Cell adhesion
- Cell adhesion/cell adhesion complex
- Cell junction
- Esterase domain
- Glycoprotein
- Lns domain
- Membrane
- Postsynaptic cell membrane
- Protein-protein complex
- Synapse
- Transmembrane
