2vh8
From Proteopedia
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|PDB= 2vh8 |SIZE=350|CAPTION= <scene name='initialview01'>2vh8</scene>, resolution 3.90Å | |PDB= 2vh8 |SIZE=350|CAPTION= <scene name='initialview01'>2vh8</scene>, resolution 3.90Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1c4r|1C4R]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vh8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vh8 OCA], [http://www.ebi.ac.uk/pdbsum/2vh8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2vh8 RCSB]</span> | ||
}} | }} | ||
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[[Category: Sulzenbacher, G.]] | [[Category: Sulzenbacher, G.]] | ||
[[Category: Taylor, P.]] | [[Category: Taylor, P.]] | ||
| - | [[Category: CA]] | ||
[[Category: alternative promoter usage]] | [[Category: alternative promoter usage]] | ||
[[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 05:12:16 2008'' |
Revision as of 02:12, 31 March 2008
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| , resolution 3.90Å | |||||||
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| Ligands: | |||||||
| Related: | 1C4R
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF SYNAPTIC PROTEIN NEUROLIGIN 4 IN COMPLEX WITH NEUREXIN BETA 1.
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
2VH8 is a Protein complex structure of sequences from Homo sapiens and Rattus norvegicus. 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 05:12:16 2008
Categories: Homo sapiens | Protein complex | Rattus norvegicus | Bourne, Y. | Comoletti, D. | Fabrichny, I P. | Leone, P. | Marchot, P. | Miller, M T. | Sulzenbacher, G. | Taylor, P. | Alternative promoter usage | Alternative splicing | Cell adhesion | Cell adhesion alpha/beta-hydrolase cholinesterase autism b | Glycoprotein | Membrane | Transmembrane
