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==Crystal Structure of Neurexin 1beta/Neuroligin 1 complex== | |||
<StructureSection load='3vkf' size='340' side='right' caption='[[3vkf]], [[Resolution|resolution]] 3.30Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3vkf]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VKF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VKF FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Nlgn1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus]), NRXN1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 Bos taurus])</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3vkf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vkf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vkf RCSB], [http://www.ebi.ac.uk/pdbsum/3vkf PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Polymorphic adhesion molecules neurexin and neuroligin (NL) mediate asymmetric trans-synaptic adhesion, which is crucial for synapse development and function. It is not known whether or how individual synapse function is controlled by the interactions between variants and isoforms of these molecules with differing ectodomain regions. At a physiological concentration of Ca(2+), the ectodomain complex of neurexin-1 beta isoform (Nrx1beta) and NL1 spontaneously assembled into crystals of a lateral sheet-like superstructure topologically compatible with transcellular adhesion. Correlative light-electron microscopy confirmed extracellular sheet formation at the junctions between Nrx1beta- and NL1-expressing non-neuronal cells, mimicking the close, parallel synaptic membrane apposition. The same NL1-expressing cells, however, did not form this higher-order architecture with cells expressing the much longer neurexin-1 alpha isoform, suggesting a functional discrimination mechanism between synaptic contacts made by different isoforms of neurexin variants. | |||
Higher-order architecture of cell adhesion mediated by polymorphic synaptic adhesion molecules neurexin and neuroligin.,Tanaka H, Miyazaki N, Matoba K, Nogi T, Iwasaki K, Takagi J Cell Rep. 2012 Jul 26;2(1):101-10. doi: 10.1016/j.celrep.2012.06.009. Epub 2012, Jul 20. PMID:22840401<ref>PMID:22840401</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== | ==See Also== | ||
*[[Neurexin|Neurexin]] | |||
*[[Neuroligin|Neuroligin]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Iwasaki, K | [[Category: Iwasaki, K]] | ||
[[Category: Miyazaki, N | [[Category: Miyazaki, N]] | ||
[[Category: Nogi, T | [[Category: Nogi, T]] | ||
[[Category: Takagi, J | [[Category: Takagi, J]] | ||
[[Category: Tanaka, H | [[Category: Tanaka, H]] | ||
[[Category: Alpha/beta hydrolase]] | [[Category: Alpha/beta hydrolase]] | ||
[[Category: Beta-sandwich]] | [[Category: Beta-sandwich]] | ||
Revision as of 09:50, 21 December 2014
Crystal Structure of Neurexin 1beta/Neuroligin 1 complexCrystal Structure of Neurexin 1beta/Neuroligin 1 complex
Structural highlights
Publication Abstract from PubMedPolymorphic adhesion molecules neurexin and neuroligin (NL) mediate asymmetric trans-synaptic adhesion, which is crucial for synapse development and function. It is not known whether or how individual synapse function is controlled by the interactions between variants and isoforms of these molecules with differing ectodomain regions. At a physiological concentration of Ca(2+), the ectodomain complex of neurexin-1 beta isoform (Nrx1beta) and NL1 spontaneously assembled into crystals of a lateral sheet-like superstructure topologically compatible with transcellular adhesion. Correlative light-electron microscopy confirmed extracellular sheet formation at the junctions between Nrx1beta- and NL1-expressing non-neuronal cells, mimicking the close, parallel synaptic membrane apposition. The same NL1-expressing cells, however, did not form this higher-order architecture with cells expressing the much longer neurexin-1 alpha isoform, suggesting a functional discrimination mechanism between synaptic contacts made by different isoforms of neurexin variants. Higher-order architecture of cell adhesion mediated by polymorphic synaptic adhesion molecules neurexin and neuroligin.,Tanaka H, Miyazaki N, Matoba K, Nogi T, Iwasaki K, Takagi J Cell Rep. 2012 Jul 26;2(1):101-10. doi: 10.1016/j.celrep.2012.06.009. Epub 2012, Jul 20. PMID:22840401[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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