3be8
From Proteopedia
(New page: 200px<br /><applet load="3be8" size="350" color="white" frame="true" align="right" spinBox="true" caption="3be8, resolution 2.20Å" /> '''Crystal structure of...) |
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==Overview== | ==Overview== | ||
| - | The neuroligins are postsynaptic cell adhesion proteins whose associations | + | 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== | ==About this Structure== | ||
| - | 3BE8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=FLC:'>FLC</scene>, <scene name='pdbligand=PO4:'>PO4</scene>, <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=NA:'>NA</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Sites: <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>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BE8 OCA]. | + | 3BE8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=FLC:'>FLC</scene>, <scene name='pdbligand=PO4:'>PO4</scene>, <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=NA:'>NA</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Sites: <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>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BE8 OCA]. |
==Reference== | ==Reference== | ||
| - | Structural | + | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18093521 18093521] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Bourne, Y.]] | [[Category: Bourne, Y.]] | ||
[[Category: Comoletti, D.]] | [[Category: Comoletti, D.]] | ||
| - | [[Category: Fabrichny, I | + | [[Category: Fabrichny, I P.]] |
[[Category: Leone, P.]] | [[Category: Leone, P.]] | ||
[[Category: Marchot, P.]] | [[Category: Marchot, P.]] | ||
| - | [[Category: Miller, M | + | [[Category: Miller, M T.]] |
[[Category: Sulzenbacher, G.]] | [[Category: Sulzenbacher, G.]] | ||
[[Category: Taylor, P.]] | [[Category: Taylor, P.]] | ||
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[[Category: transmembrane]] | [[Category: transmembrane]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:05:13 2008'' |
Revision as of 17:05, 21 February 2008
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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 with , , , , and as ligands. Known structural/functional Sites: , , , , , , , , , , , , , and . 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 Thu Feb 21 19:05:13 2008
Categories: Homo sapiens | Single protein | Bourne, Y. | Comoletti, D. | Fabrichny, I P. | Leone, P. | Marchot, P. | Miller, M T. | Sulzenbacher, G. | Taylor, P. | CL | FLC | GOL | NA | NAG | PO4 | A/b-hydrolase fold | Alternative splicing | Cell adhesion protein | Four-helix bundle | Glycoprotein | Membrane | Neuroligin | Polymorphism | Synaptic protein | Transmembrane
