3bl8

From Proteopedia

(Difference between revisions)

Revision as of 21:04, 25 December 2014

Crystal structure of the extracellular domain of neuroligin 2A from mouse

Structural highlights

3bl8 is a 4 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Gene:	Nlgn2, Kiaa1366 (Mus musculus)
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[NLGN2_MOUSE] Transmembrane scaffolding protein involved in cell-cell interactions via its interactions with neurexin family members. Mediates cell-cell interactions both in neurons and in other types of cells, such as Langerhans beta cells. Mediates cell-cell interactions between Langerhans beta cells and modulates insulin secretion (By similarity). Plays a role in synapse function and synaptic signal transmission, especially via gamma-aminobutyric acid receptors (GABA(A) receptors). Functions by recruiting and clustering synaptic proteins. Promotes clustering of postsynaptic GABRG2 and GPHN. Modulates signaling by inhibitory synapses, and thereby plays a role in controlling the ratio of signaling by excitatory and inhibitory synapses and information processing. Required for normal signal amplitude from inhibitory synapses, but is not essential for normal signal frequency. May promote the initial formation of synapses, but is not essential for this. In vitro, triggers the de novo formation of presynaptic structures.^[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

Neuroligins (NLs) are catalytically inactive members of a family of cholinesterase-like transmembrane proteins that mediate cell adhesion at neuronal synapses. Postsynaptic neuroligins engage in Ca2+-dependent transsynaptic interactions via their extracellular cholinesterase domain with presynaptic neurexins (NRXs). These interactions may be regulated by two short splice insertions (termed A and B) in the NL cholinesterase domain. Here, we present the 3.3-A crystal structure of the ectodomain from NL2 containing splice insertion A (NL2A). The overall structure of NL2A resembles that of cholinesterases, but several structural features are unique to the NL proteins. First, structural elements surrounding the esterase active-site region differ significantly between active esterases and NL2A. On the opposite surface of the NL2A molecule, the positions of the A and B splice insertions identify a candidate NRX interaction site of the NL protein. Finally, sequence comparisons of NL isoforms allow for mapping the location of residues of previously identified mutations in NL3 and NL4 found in patients with autism spectrum disorders. Overall, the NL2 structure promises to provide a valuable model for dissecting NL isoform- and synapse-specific functions.

Crystal structure of the extracellular cholinesterase-like domain from neuroligin-2.,Koehnke J, Jin X, Budreck EC, Posy S, Scheiffele P, Honig B, Shapiro L Proc Natl Acad Sci U S A. 2008 Feb 12;105(6):1873-8. Epub 2008 Feb 4. PMID:18250328^[7]

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

References

↑ Scheiffele P, Fan J, Choih J, Fetter R, Serafini T. Neuroligin expressed in nonneuronal cells triggers presynaptic development in contacting axons. Cell. 2000 Jun 9;101(6):657-69. PMID:10892652
↑ 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
↑ Varoqueaux F, Aramuni G, Rawson RL, Mohrmann R, Missler M, Gottmann K, Zhang W, Sudhof TC, Brose N. Neuroligins determine synapse maturation and function. Neuron. 2006 Sep 21;51(6):741-54. PMID:16982420 doi:http://dx.doi.org/10.1016/j.neuron.2006.09.003
↑ Hoon M, Bauer G, Fritschy JM, Moser T, Falkenburger BH, Varoqueaux F. Neuroligin 2 controls the maturation of GABAergic synapses and information processing in the retina. J Neurosci. 2009 Jun 24;29(25):8039-50. doi: 10.1523/JNEUROSCI.0534-09.2009. PMID:19553444 doi:http://dx.doi.org/10.1523/JNEUROSCI.0534-09.2009
↑ Gibson JR, Huber KM, Sudhof TC. Neuroligin-2 deletion selectively decreases inhibitory synaptic transmission originating from fast-spiking but not from somatostatin-positive interneurons. J Neurosci. 2009 Nov 4;29(44):13883-97. doi: 10.1523/JNEUROSCI.2457-09.2009. PMID:19889999 doi:http://dx.doi.org/10.1523/JNEUROSCI.2457-09.2009
↑ Jedlicka P, Hoon M, Papadopoulos T, Vlachos A, Winkels R, Poulopoulos A, Betz H, Deller T, Brose N, Varoqueaux F, Schwarzacher SW. Increased dentate gyrus excitability in neuroligin-2-deficient mice in vivo. Cereb Cortex. 2011 Feb;21(2):357-67. doi: 10.1093/cercor/bhq100. Epub 2010 Jun 7. PMID:20530218 doi:http://dx.doi.org/10.1093/cercor/bhq100
↑ Koehnke J, Jin X, Budreck EC, Posy S, Scheiffele P, Honig B, Shapiro L. Crystal structure of the extracellular cholinesterase-like domain from neuroligin-2. Proc Natl Acad Sci U S A. 2008 Feb 12;105(6):1873-8. Epub 2008 Feb 4. PMID:18250328

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3bl8"

@@ Line 3: / Line 3: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[3bl8]] is a 4 chain structure with 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=3BL8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3BL8 FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene><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=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr>
-<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Nlgn2, Kiaa1366 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Nlgn2, Kiaa1366 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])</td></tr>
-<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3bl8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bl8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3bl8 RCSB], [http://www.ebi.ac.uk/pdbsum/3bl8 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=3bl8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bl8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3bl8 RCSB], [http://www.ebi.ac.uk/pdbsum/3bl8 PDBsum]</span></td></tr>
-<table>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/NLGN2_MOUSE NLGN2_MOUSE]] Transmembrane scaffolding protein involved in cell-cell interactions via its interactions with neurexin family members. Mediates cell-cell interactions both in neurons and in other types of cells, such as Langerhans beta cells. Mediates cell-cell interactions between Langerhans beta cells and modulates insulin secretion (By similarity). Plays a role in synapse function and synaptic signal transmission, especially via gamma-aminobutyric acid receptors (GABA(A) receptors). Functions by recruiting and clustering synaptic proteins. Promotes clustering of postsynaptic GABRG2 and GPHN. Modulates signaling by inhibitory synapses, and thereby plays a role in controlling the ratio of signaling by excitatory and inhibitory synapses and information processing. Required for normal signal amplitude from inhibitory synapses, but is not essential for normal signal frequency. May promote the initial formation of synapses, but is not essential for this. In vitro, triggers the de novo formation of presynaptic structures.<ref>PMID:10892652</ref> <ref>PMID:15620359</ref> <ref>PMID:16982420</ref> <ref>PMID:19553444</ref> <ref>PMID:19889999</ref> <ref>PMID:20530218</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 33: / Line 35: @@
 </StructureSection>
 [[Category: Mus musculus]]
-[[Category: Jin, X.]]
+[[Category: Jin, X]]
-[[Category: Koehnke, J.]]
+[[Category: Koehnke, J]]
-[[Category: Shapiro, L.]]
+[[Category: Shapiro, L]]
 [[Category: Cell adhesion]]
 [[Category: Glycoprotein]]

3bl8

From Proteopedia

Revision as of 21:04, 25 December 2014

Crystal structure of the extracellular domain of neuroligin 2A from mouse

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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