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- | {{Seed}} | |
- | [[Image:3bod.png|left|200px]] | |
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- | <!--
| + | ==Structure of mouse beta-neurexin 1== |
- | The line below this paragraph, containing "STRUCTURE_3bod", creates the "Structure Box" on the page.
| + | <StructureSection load='3bod' size='340' side='right'caption='[[3bod]], [[Resolution|resolution]] 1.70Å' scene=''> |
- | You may change the PDB parameter (which sets the PDB file loaded into the applet)
| + | == Structural highlights == |
- | or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
| + | <table><tr><td colspan='2'>[[3bod]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BOD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BOD FirstGlance]. <br> |
- | or leave the SCENE parameter empty for the default display. | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> |
- | --> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> |
- | {{STRUCTURE_3bod| PDB=3bod | SCENE= }}
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3bod FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bod OCA], [https://pdbe.org/3bod PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bod RCSB], [https://www.ebi.ac.uk/pdbsum/3bod PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bod ProSAT]</span></td></tr> |
| + | </table> |
| + | == Function == |
| + | [https://www.uniprot.org/uniprot/NRX1A_MOUSE 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.<ref>PMID:9430716</ref> <ref>PMID:12827191</ref> <ref>PMID:14983056</ref> <ref>PMID:17035546</ref> <ref>PMID:16406382</ref> <ref>PMID:21410790</ref> |
| + | == Evolutionary Conservation == |
| + | [[Image:Consurf_key_small.gif|200px|right]] |
| + | Check<jmol> |
| + | <jmolCheckbox> |
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bo/3bod_consurf.spt"</scriptWhenChecked> |
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| + | <text>to colour the structure by Evolutionary Conservation</text> |
| + | </jmolCheckbox> |
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3bod ConSurf]. |
| + | <div style="clear:both"></div> |
| | | |
- | ===Structure of mouse beta-neurexin 1=== | + | ==See Also== |
- | | + | *[[Neurexin|Neurexin]] |
- | | + | == References == |
- | <!-- | + | <references/> |
- | The line below this paragraph, {{ABSTRACT_PUBMED_18334216}}, adds the Publication Abstract to the page
| + | __TOC__ |
- | (as it appears on PubMed at http://www.pubmed.gov), where 18334216 is the PubMed ID number.
| + | </StructureSection> |
- | -->
| + | [[Category: Large Structures]] |
- | {{ABSTRACT_PUBMED_18334216}}
| + | |
- | | + | |
- | ==About this Structure==
| + | |
- | 3BOD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BOD OCA].
| + | |
- | | + | |
- | ==Reference==
| + | |
- | 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:[http://www.ncbi.nlm.nih.gov/pubmed/18334216 18334216]
| + | |
| [[Category: Mus musculus]] | | [[Category: Mus musculus]] |
- | [[Category: Single protein]]
| + | [[Category: Jin X]] |
- | [[Category: Jin, X.]] | + | [[Category: Koehnke J]] |
- | [[Category: Koehnke, J.]] | + | [[Category: Shapiro L]] |
- | [[Category: Shapiro, L.]] | + | |
- | [[Category: Alternative splicing]]
| + | |
- | [[Category: Calcium]]
| + | |
- | [[Category: Cell adhesion]]
| + | |
- | [[Category: Egf-like domain]]
| + | |
- | [[Category: Glycoprotein]]
| + | |
- | [[Category: Lns6]]
| + | |
- | [[Category: Membrane]]
| + | |
- | [[Category: Metal-binding]]
| + | |
- | [[Category: Neurexin1d]]
| + | |
- | [[Category: Transmembrane]]
| + | |
- | | + | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 08:47:34 2008''
| + | |
| Structural highlights
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.
See Also
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
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