3be8
From Proteopedia
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|PDB= 3be8 |SIZE=350|CAPTION= <scene name='initialview01'>3be8</scene>, resolution 2.20Å | |PDB= 3be8 |SIZE=350|CAPTION= <scene name='initialview01'>3be8</scene>, resolution 2.20Å | ||
|SITE= <scene name='pdbsite=AC1:Nag+Binding+Site+For+Residue+A+621'>AC1</scene>, <scene name='pdbsite=AC2:Nag+Binding+Site+For+Residue+B+621'>AC2</scene>, <scene name='pdbsite=AC3:Flc+Binding+Site+For+Residue+A+622'>AC3</scene>, <scene name='pdbsite=AC4:Po4+Binding+Site+For+Residue+A+623'>AC4</scene>, <scene name='pdbsite=AC5:Cl+Binding+Site+For+Residue+A+624'>AC5</scene>, <scene name='pdbsite=AC6:Cl+Binding+Site+For+Residue+A+625'>AC6</scene>, <scene name='pdbsite=AC7:Na+Binding+Site+For+Residue+A+626'>AC7</scene>, <scene name='pdbsite=AC8:Cl+Binding+Site+For+Residue+A+627'>AC8</scene>, <scene name='pdbsite=AC9:Cl+Binding+Site+For+Residue+B+622'>AC9</scene>, <scene name='pdbsite=BC1:Flc+Binding+Site+For+Residue+B+623'>BC1</scene>, <scene name='pdbsite=BC2:Po4+Binding+Site+For+Residue+B+624'>BC2</scene>, <scene name='pdbsite=BC3:Cl+Binding+Site+For+Residue+B+625'>BC3</scene>, <scene name='pdbsite=BC4:Cl+Binding+Site+For+Residue+B+626'>BC4</scene>, <scene name='pdbsite=BC5:Gol+Binding+Site+For+Residue+A+628'>BC5</scene> and <scene name='pdbsite=BC6:Gol+Binding+Site+For+Residue+B+627'>BC6</scene> | |SITE= <scene name='pdbsite=AC1:Nag+Binding+Site+For+Residue+A+621'>AC1</scene>, <scene name='pdbsite=AC2:Nag+Binding+Site+For+Residue+B+621'>AC2</scene>, <scene name='pdbsite=AC3:Flc+Binding+Site+For+Residue+A+622'>AC3</scene>, <scene name='pdbsite=AC4:Po4+Binding+Site+For+Residue+A+623'>AC4</scene>, <scene name='pdbsite=AC5:Cl+Binding+Site+For+Residue+A+624'>AC5</scene>, <scene name='pdbsite=AC6:Cl+Binding+Site+For+Residue+A+625'>AC6</scene>, <scene name='pdbsite=AC7:Na+Binding+Site+For+Residue+A+626'>AC7</scene>, <scene name='pdbsite=AC8:Cl+Binding+Site+For+Residue+A+627'>AC8</scene>, <scene name='pdbsite=AC9:Cl+Binding+Site+For+Residue+B+622'>AC9</scene>, <scene name='pdbsite=BC1:Flc+Binding+Site+For+Residue+B+623'>BC1</scene>, <scene name='pdbsite=BC2:Po4+Binding+Site+For+Residue+B+624'>BC2</scene>, <scene name='pdbsite=BC3:Cl+Binding+Site+For+Residue+B+625'>BC3</scene>, <scene name='pdbsite=BC4:Cl+Binding+Site+For+Residue+B+626'>BC4</scene>, <scene name='pdbsite=BC5:Gol+Binding+Site+For+Residue+A+628'>BC5</scene> and <scene name='pdbsite=BC6:Gol+Binding+Site+For+Residue+B+627'>BC6</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= NLGN4X ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= NLGN4X ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3be8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3be8 OCA], [http://www.ebi.ac.uk/pdbsum/3be8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3be8 RCSB]</span> | ||
}} | }} | ||
| Line 30: | Line 33: | ||
[[Category: Sulzenbacher, G.]] | [[Category: Sulzenbacher, G.]] | ||
[[Category: Taylor, P.]] | [[Category: Taylor, P.]] | ||
| - | [[Category: CL]] | ||
| - | [[Category: FLC]] | ||
| - | [[Category: GOL]] | ||
| - | [[Category: NA]] | ||
| - | [[Category: NAG]] | ||
| - | [[Category: PO4]] | ||
[[Category: a/b-hydrolase fold]] | [[Category: a/b-hydrolase fold]] | ||
[[Category: alternative splicing]] | [[Category: alternative splicing]] | ||
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[[Category: transmembrane]] | [[Category: transmembrane]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:25:28 2008'' |
Revision as of 02:25, 31 March 2008
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| , resolution 2.20Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , , , , , , , , , , , , and | ||||||
| Ligands: | , , , , , | ||||||
| Gene: | NLGN4X (Homo sapiens) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the synaptic protein neuroligin 4
Overview
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.
About this Structure
3BE8 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Mon Mar 31 05:25:28 2008
Categories: Homo sapiens | Single protein | Bourne, Y. | Comoletti, D. | Fabrichny, I P. | Leone, P. | Marchot, P. | Miller, M T. | Sulzenbacher, G. | Taylor, P. | A/b-hydrolase fold | Alternative splicing | Cell adhesion protein | Four-helix bundle | Glycoprotein | Membrane | Neuroligin | Polymorphism | Synaptic protein | Transmembrane
