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3bod

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Revision as of 02:16, 16 November 2017

Structure of mouse beta-neurexin 1

Structural highlights

3bod is a 1 chain structure with sequence from Lk3 transgenic mice. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:	Nrxn1, Kiaa0578 (LK3 transgenic mice)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[NRX1A_MOUSE] Cell surface protein involved in cell-cell-interactions, exocytosis of secretory granules and regulation of signal transmission. Function is isoform-specific. Alpha-type isoforms have a long N-terminus with six laminin G-like domains and play an important role in synaptic signal transmission. Alpha-type isoforms play a role in the regulation of calcium channel activity and Ca(2+)-triggered neurotransmitter release at synapses and at neuromuscular junctions. They play an important role in Ca(2+)-triggered exocytosis of secretory granules in pituitary gland. They may effect their functions at synapses and in endocrine cells via their interactions with proteins from the exocytotic machinery. Likewise, alpha-type isoforms play a role in regulating the activity of postsynaptic NMDA receptors, a subtype of glutamate-gated ion channels. Both alpha-type and beta-type isoforms may play a role in the formation or maintenance of synaptic junctions via their interactions (via the extracellular domains) with neuroligin family members, CBLN1 or CBLN2. In vitro, triggers the de novo formation of presynaptic structures. May be involved in specification of excitatory synapses. Alpha-type isoforms were first identified as receptors for alpha-latrotoxin from spider venom.^[1] ^[2] ^[3] ^[4] ^[5] ^[6]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Presynaptic neurexins (NRXs) bind to postsynaptic neuroligins (NLs) to form Ca(2+)-dependent complexes that bridge neural synapses. beta-NRXs bind NLs through their LNS domains, which contain a single site of alternative splicing (splice site 4) giving rise to two isoforms: +4 and Delta. We present crystal structures of the Delta isoforms of the LNS domains from beta-NRX1 and beta-NRX2, crystallized in the presence of Ca(2+) ions. The Ca(2+)-binding site is disordered in the beta-NRX2 structure, but the 1.7 A beta-NRX1 structure reveals a single Ca(2+) ion, approximately 12 A from the splice insertion site, with one coordinating ligand donated by a glutamic acid from an adjacent beta-NRX1 molecule. NMR studies of beta-NRX1+4 show that the insertion sequence is unstructured, and remains at least partially disordered in complex with NL. These results raise the possibility that beta-NRX insertion sequence 4 may function in roles independent of neuroligin binding.

Crystal structures of beta-neurexin 1 and beta-neurexin 2 ectodomains and dynamics of splice insertion sequence 4.,Koehnke J, Jin X, Trbovic N, Katsamba PS, Brasch J, Ahlsen G, Scheiffele P, Honig B, Palmer AG 3rd, Shapiro L Structure. 2008 Mar;16(3):410-21. PMID:18334216^[7]

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

References

↑ Geppert M, Khvotchev M, Krasnoperov V, Goda Y, Missler M, Hammer RE, Ichtchenko K, Petrenko AG, Sudhof TC. Neurexin I alpha is a major alpha-latrotoxin receptor that cooperates in alpha-latrotoxin action. J Biol Chem. 1998 Jan 16;273(3):1705-10. PMID:9430716
↑ Missler M, Zhang W, Rohlmann A, Kattenstroth G, Hammer RE, Gottmann K, Sudhof TC. Alpha-neurexins couple Ca2+ channels to synaptic vesicle exocytosis. Nature. 2003 Jun 26;423(6943):939-48. PMID:12827191 doi:http://dx.doi.org/10.1038/nature01755
↑ Kattenstroth G, Tantalaki E, Sudhof TC, Gottmann K, Missler M. Postsynaptic N-methyl-D-aspartate receptor function requires alpha-neurexins. Proc Natl Acad Sci U S A. 2004 Feb 24;101(8):2607-12. PMID:14983056
↑ Dudanova I, Sedej S, Ahmad M, Masius H, Sargsyan V, Zhang W, Riedel D, Angenstein F, Schild D, Rupnik M, Missler M. Important contribution of alpha-neurexins to Ca2+-triggered exocytosis of secretory granules. J Neurosci. 2006 Oct 11;26(41):10599-613. PMID:17035546 doi:http://dx.doi.org/10.1523/JNEUROSCI.1913-06.2006
↑ Sons MS, Busche N, Strenzke N, Moser T, Ernsberger U, Mooren FC, Zhang W, Ahmad M, Steffens H, Schomburg ED, Plomp JJ, Missler M. alpha-Neurexins are required for efficient transmitter release and synaptic homeostasis at the mouse neuromuscular junction. Neuroscience. 2006;138(2):433-46. Epub 2006 Jan 10. PMID:16406382 doi:http://dx.doi.org/10.1016/j.neuroscience.2005.11.040
↑ Matsuda K, Yuzaki M. Cbln family proteins promote synapse formation by regulating distinct neurexin signaling pathways in various brain regions. Eur J Neurosci. 2011 Apr;33(8):1447-61. doi: 10.1111/j.1460-9568.2011.07638.x., Epub 2011 Mar 17. PMID:21410790 doi:http://dx.doi.org/10.1111/j.1460-9568.2011.07638.x
↑ Koehnke J, Jin X, Trbovic N, Katsamba PS, Brasch J, Ahlsen G, Scheiffele P, Honig B, Palmer AG 3rd, Shapiro L. Crystal structures of beta-neurexin 1 and beta-neurexin 2 ectodomains and dynamics of splice insertion sequence 4. Structure. 2008 Mar;16(3):410-21. PMID:18334216 doi:10.1016/j.str.2007.12.024

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 1: / Line 1: @@
 ==Structure of mouse beta-neurexin 1==
 <StructureSection load='3bod' size='340' side='right' caption='[[3bod]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Nrxn1, Kiaa0578 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=3bod FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bod OCA], [http://pdbe.org/3bod PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3bod RCSB], [http://www.ebi.ac.uk/pdbsum/3bod PDBsum]</span></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=3bod FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bod OCA], [http://pdbe.org/3bod PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3bod RCSB], [http://www.ebi.ac.uk/pdbsum/3bod PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3bod ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 28: / Line 29: @@
 </div>
 <div class="pdbe-citations 3bod" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Neurexin|Neurexin]]
 == References ==
 <references/>
@@ Line 39: / Line 37: @@
 [[Category: Koehnke, J]]
 [[Category: Shapiro, L]]
+[[Category: Alternative splicing]]
+[[Category: Calcium]]
 [[Category: Cell adhesion]]
 [[Category: Egf-like domain]]

3bod

From Proteopedia

Revision as of 02:16, 16 November 2017

Structure of mouse beta-neurexin 1

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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