3be8: Difference between revisions

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New page: left|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, 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 Ca(2+)-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.
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 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]
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.P.]]
[[Category: Fabrichny, I P.]]
[[Category: Leone, P.]]
[[Category: Leone, P.]]
[[Category: Marchot, P.]]
[[Category: Marchot, P.]]
[[Category: Miller, M.T.]]
[[Category: Miller, M T.]]
[[Category: Sulzenbacher, G.]]
[[Category: Sulzenbacher, G.]]
[[Category: Taylor, P.]]
[[Category: Taylor, P.]]
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[[Category: transmembrane]]
[[Category: transmembrane]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:05:13 2008''