2wqz

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of synaptic protein neuroligin-4 in complex with neurexin-beta 1: alternative refinement

Structural highlights

2wqz is a 4 chain structure with sequence from Homo sapiens and Rattus norvegicus. This structure supersedes the now removed PDB entry 2vh8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3.9Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

NLGNX_HUMAN Defects in NLGN4X may be the cause of susceptibility to autism X-linked type 2 (AUTSX2) [MIM:300495. AUTSX2 is a pervasive developmental disorder (PDD), prototypically characterized by impairments in reciprocal social interaction and communication, restricted and stereotyped patterns of interests and activities, and the presence of developmental abnormalities by 3 years of age.^[1] Defects in NLGN4X may be the cause of susceptibility to X-linked Asperger syndrome 2 (ASPGX2) [MIM:300497. ASPGX2 is considered to be a form of childhood autism.

Function

NLGNX_HUMAN Putative neuronal cell surface protein involved in cell-cell-interactions.

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

The neuroligins are postsynaptic cell adhesion proteins whose associations with presynaptic neurexins participate in synaptogenesis. Mutations in the neuroligin and neurexin genes appear to be associated with autism and mental retardation. The crystal structure of a neuroligin reveals features not found in its catalytically active relatives, such as the fully hydrophobic interface forming the functional neuroligin dimer; the conformations of surface loops surrounding the vestigial active center; the location of determinants that are critical for folding and processing; and the absence of a macromolecular dipole and presence of an electronegative, hydrophilic surface for neurexin binding. The structure of a beta-neurexin-neuroligin complex reveals the precise orientation of the bound neurexin and, despite a limited resolution, provides substantial information on the Ca2+-dependent interactions network involved in trans-synaptic neurexin-neuroligin association. These structures exemplify how an alpha/beta-hydrolase fold varies in surface topography to confer adhesion properties and provide templates for analyzing abnormal processing or recognition events associated with autism.

Structural analysis of the synaptic protein neuroligin and its beta-neurexin complex: determinants for folding and cell adhesion.,Fabrichny IP, Leone P, Sulzenbacher G, Comoletti D, Miller MT, Taylor P, Bourne Y, Marchot P Neuron. 2007 Dec 20;56(6):979-91. PMID:18093521^[2]

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

References

↑ Jamain S, Quach H, Betancur C, Rastam M, Colineaux C, Gillberg IC, Soderstrom H, Giros B, Leboyer M, Gillberg C, Bourgeron T. Mutations of the X-linked genes encoding neuroligins NLGN3 and NLGN4 are associated with autism. Nat Genet. 2003 May;34(1):27-9. PMID:12669065 doi:10.1038/ng1136
↑ Fabrichny IP, Leone P, Sulzenbacher G, Comoletti D, Miller MT, Taylor P, Bourne Y, Marchot P. Structural analysis of the synaptic protein neuroligin and its beta-neurexin complex: determinants for folding and cell adhesion. Neuron. 2007 Dec 20;56(6):979-91. PMID:18093521 doi:10.1016/j.neuron.2007.11.013

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2wqz"

@@ Line 1: / Line 1: @@
 ==Crystal structure of synaptic protein neuroligin-4 in complex with neurexin-beta 1: alternative refinement==
-<StructureSection load='2wqz' size='340' side='right' caption='[[2wqz]], [[Resolution|resolution]] 3.90&Aring;' scene=''>
+<StructureSection load='2wqz' size='340' side='right'caption='[[2wqz]], [[Resolution|resolution]] 3.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2wqz]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat] and [http://en.wikipedia.org/wiki/Human Human]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2vh8 2vh8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WQZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2WQZ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2wqz]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2vh8 2vh8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WQZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WQZ 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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.9&#8491;</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=2wqz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wqz OCA], [http://pdbe.org/2wqz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2wqz RCSB], [http://www.ebi.ac.uk/pdbsum/2wqz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2wqz ProSAT]</span></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>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2wqz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wqz OCA], [https://pdbe.org/2wqz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wqz RCSB], [https://www.ebi.ac.uk/pdbsum/2wqz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wqz ProSAT]</span></td></tr>
 </table>
+== Disease ==
+[https://www.uniprot.org/uniprot/NLGNX_HUMAN NLGNX_HUMAN] Defects in NLGN4X may be the cause of susceptibility to autism X-linked type 2 (AUTSX2) [MIM:[https://omim.org/entry/300495 300495]. AUTSX2 is a pervasive developmental disorder (PDD), prototypically characterized by impairments in reciprocal social interaction and communication, restricted and stereotyped patterns of interests and activities, and the presence of developmental abnormalities by 3 years of age.<ref>PMID:12669065</ref>   Defects in NLGN4X may be the cause of susceptibility to X-linked Asperger syndrome 2 (ASPGX2) [MIM:[https://omim.org/entry/300497 300497]. ASPGX2 is considered to be a form of childhood autism.
 == Function ==
-[[http://www.uniprot.org/uniprot/NRX1B_RAT NRX1B_RAT]] 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).<ref>PMID:9325340</ref>
+[https://www.uniprot.org/uniprot/NLGNX_HUMAN NLGNX_HUMAN] Putative neuronal cell surface protein involved in cell-cell-interactions.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 32: / Line 35: @@
 *[[Neurexin|Neurexin]]
 *[[Neuroligin|Neuroligin]]
-*[[Neuroligin-Neurexin Interaction|Neuroligin-Neurexin Interaction]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Buffalo rat]]
+[[Category: Homo sapiens]]
-[[Category: Human]]
+[[Category: Large Structures]]
-[[Category: Bourne, Y]]
+[[Category: Rattus norvegicus]]
-[[Category: Comoletti, D]]
+[[Category: Bourne Y]]
-[[Category: Fabrichny, I P]]
+[[Category: Comoletti D]]
-[[Category: Leone, P]]
+[[Category: Fabrichny IP]]
-[[Category: Marchot, P]]
+[[Category: Leone P]]
-[[Category: Miller, M T]]
+[[Category: Marchot P]]
-[[Category: Sulzenbacher, G]]
+[[Category: Miller MT]]
-[[Category: Taylor, P]]
+[[Category: Sulzenbacher G]]
-[[Category: Alpha/beta-hydrolase cholinesterase autism brain]]
+[[Category: Taylor P]]
-[[Category: Alternative promoter usage]]
-[[Category: Cell adhesion]]
-[[Category: Disulfide bond]]
-[[Category: Glycoprotein]]
-[[Category: Membrane]]
-[[Category: Transmembrane]]

2wqz

From Proteopedia

Current revision

Crystal structure of synaptic protein neuroligin-4 in complex with neurexin-beta 1: alternative refinement

Structural highlights

Disease

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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