3asi: Difference between revisions
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[[ | ==Alpha-Neurexin-1 ectodomain fragment; LNS5-EGF3-LNS6== | ||
<StructureSection load='3asi' size='340' side='right' caption='[[3asi]], [[Resolution|resolution]] 2.30Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3asi]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ASI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ASI FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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">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=3asi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3asi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3asi RCSB], [http://www.ebi.ac.uk/pdbsum/3asi PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. alpha-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 beta-Nrx has but a single LNS domain. It has long been known that the larger alpha-Nrx and the shorter beta-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 Nrx1alpha ectodomain, consisting of LNS5-EGF3-LNS6. The 2.3 A-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 alpha-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 alpha-Nrx. This, combined with a low-resolution molecular envelope obtained by a single particle reconstruction performed on negatively stained full-length Nrx1alpha sample, allowed us to derive a structural model of the alpha-Nrx ectodomain. This model will help us understand not only how the large alpha-Nrx ectodomain is accommodated in the synaptic cleft, but also how the trans-synaptic adhesion mediated by alpha- and beta-Nrxs could differentially affect synaptic structure and function. | |||
Structural Basis for Variant-Specific Neuroligin-Binding by alpha-Neurexin.,Tanaka H, Nogi T, Yasui N, Iwasaki K, Takagi J PLoS One. 2011 Apr 28;6(4):e19411. PMID:21552542<ref>PMID:21552542</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Neurexin|Neurexin]] | *[[Neurexin|Neurexin]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Nogi, T.]] | [[Category: Nogi, T.]] | ||
