3vkf

From Proteopedia

(Difference between revisions)

Revision as of 01:44, 25 December 2014

Crystal Structure of Neurexin 1beta/Neuroligin 1 complex

Structural highlights

3vkf is a 4 chain structure with sequence from Bos taurus and Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Gene:	Nlgn1 (Rattus norvegicus), NRXN1 (Bos taurus)
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[NLGN1_RAT] Cell surface protein involved in cell-cell-interactions via its interactions with neurexin family members. Plays a role in synapse function and synaptic signal transmission, and probably mediates its effects by recruiting and clustering other synaptic proteins. May promote the initial formation of synapses, but is not essential for this. In vitro, triggers the de novo formation of presynaptic structures. May be involved in specification of excitatory synapses.^[1] ^[2] [NRX1B_BOVIN] Neuronal cell surface protein that may be involved in cell recognition and cell adhesion by forming intracellular junctions through binding to neuroligins. May play a role in formation or maintenance of synaptic junctions. May mediate intracellular signaling. May play a role in angiogenesis (By similarity).

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^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Nguyen T, Sudhof TC. Binding properties of neuroligin 1 and neurexin 1beta reveal function as heterophilic cell adhesion molecules. J Biol Chem. 1997 Oct 10;272(41):26032-9. PMID:9325340
↑ Graf ER, Zhang X, Jin SX, Linhoff MW, Craig AM. Neurexins induce differentiation of GABA and glutamate postsynaptic specializations via neuroligins. Cell. 2004 Dec 29;119(7):1013-26. PMID:15620359 doi:10.1016/j.cell.2004.11.035
↑ Tanaka H, Miyazaki N, Matoba K, Nogi T, Iwasaki K, Takagi J. Higher-order architecture of cell adhesion mediated by polymorphic synaptic adhesion molecules neurexin and neuroligin. Cell Rep. 2012 Jul 26;2(1):101-10. doi: 10.1016/j.celrep.2012.06.009. Epub 2012, Jul 20. PMID:22840401 doi:10.1016/j.celrep.2012.06.009

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3vkf"

@@ Line 7: / Line 7: @@
 <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>
+== Function ==
+[[http://www.uniprot.org/uniprot/NLGN1_RAT NLGN1_RAT]] Cell surface protein involved in cell-cell-interactions via its interactions with neurexin family members. Plays a role in synapse function and synaptic signal transmission, and probably mediates its effects by recruiting and clustering other synaptic proteins. May promote the initial formation of synapses, but is not essential for this. In vitro, triggers the de novo formation of presynaptic structures. May be involved in specification of excitatory synapses.<ref>PMID:9325340</ref> <ref>PMID:15620359</ref>  [[http://www.uniprot.org/uniprot/NRX1B_BOVIN NRX1B_BOVIN]] Neuronal cell surface protein that may be involved in cell recognition and cell adhesion by forming intracellular junctions through binding to neuroligins. May play a role in formation or maintenance of synaptic junctions. May mediate intracellular signaling. May play a role in angiogenesis (By similarity).
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

3vkf

From Proteopedia

Revision as of 01:44, 25 December 2014

Crystal Structure of Neurexin 1beta/Neuroligin 1 complex

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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