This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
3bix
From Proteopedia
(New page: 200px<br /><applet load="3bix" size="450" color="white" frame="true" align="right" spinBox="true" caption="3bix, resolution 1.800Å" /> '''Crystal structure o...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:3bix.jpg|left|200px]]<br /><applet load="3bix" size=" | + | [[Image:3bix.jpg|left|200px]]<br /><applet load="3bix" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="3bix, resolution 1.800Å" /> | caption="3bix, resolution 1.800Å" /> | ||
'''Crystal structure of the extracellular esterase domain of Neuroligin-1'''<br /> | '''Crystal structure of the extracellular esterase domain of Neuroligin-1'''<br /> | ||
| Line 7: | Line 7: | ||
==About this Structure== | ==About this Structure== | ||
| - | 3BIX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=NAG: | + | 3BIX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=NI:'>NI</scene> and <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BIX OCA]. |
==Reference== | ==Reference== | ||
| Line 34: | Line 34: | ||
[[Category: transmembrane]] | [[Category: transmembrane]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 11:14:12 2008'' |
Revision as of 09:14, 23 January 2008
|
Crystal structure of the extracellular esterase domain of Neuroligin-1
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
3BIX is a Single protein structure of sequence from Rattus norvegicus with , and 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
Page seeded by OCA on Wed Jan 23 11:14:12 2008
Categories: Rattus norvegicus | Single protein | Arac, D. | Boucard, A.A. | Brunger, A.T. | Newell, E. | Ozkan, E. | Strop, P. | Sudhof, T.C. | EDO | NAG | NI | Alpha-beta hydrolase | Alternative splicing | Cell adhesion | Cell junction | Esterase domain | Glycoprotein | Membrane | Postsynaptic cell membrane | Synapse | Transmembrane
