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3b3q
From Proteopedia
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| - | [[Image:3b3q.jpg|left|200px]] | + | [[Image:3b3q.jpg|left|200px]] |
| - | + | ||
| - | '''Crystal structure of a synaptic adhesion complex''' | + | {{Structure |
| + | |PDB= 3b3q |SIZE=350|CAPTION= <scene name='initialview01'>3b3q</scene>, resolution 2.4Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> and <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= Nlgn1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]), NRXN1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of a synaptic adhesion complex''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 3B3Q is a [ | + | 3B3Q is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3B3Q OCA]. |
==Reference== | ==Reference== | ||
| - | Structural basis for synaptic adhesion mediated by neuroligin-neurexin interactions., Chen X, Liu H, Shim AH, Focia PJ, He X, Nat Struct Mol Biol. 2008 Jan;15(1):50-6. Epub 2007 Dec 16. PMID:[http:// | + | Structural basis for synaptic adhesion mediated by neuroligin-neurexin interactions., Chen X, Liu H, Shim AH, Focia PJ, He X, Nat Struct Mol Biol. 2008 Jan;15(1):50-6. Epub 2007 Dec 16. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18084303 18084303] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
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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 Mar 20 18:55:51 2008'' |
Revision as of 16:55, 20 March 2008
| |||||||
| , resolution 2.4Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Gene: | Nlgn1 (Mus musculus), NRXN1 (Homo sapiens) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of a synaptic adhesion complex
Overview
The heterophilic synaptic adhesion molecules neuroligins and neurexins are essential for establishing and maintaining neuronal circuits by modulating the formation and maturation of synapses. The neuroligin-neurexin adhesion is Ca2+-dependent and regulated by alternative splicing. We report a structure of the complex at a resolution of 2.4 A between the mouse neuroligin-1 (NL1) cholinesterase-like domain and the mouse neurexin-1beta (NX1beta) LNS (laminin, neurexin and sex hormone-binding globulin-like) domain. The structure revealed a delicate neuroligin-neurexin assembly mediated by a hydrophilic, Ca2+-mediated and solvent-supplemented interface, rendering it capable of being modulated by alternative splicing and other regulatory factors. Thermodynamic data supported a mechanism wherein splicing site B of NL1 acts by modulating a salt bridge at the edge of the NL1-NX1beta interface. Mapping neuroligin mutations implicated in autism indicated that most such mutations are structurally destabilizing, supporting deficient neuroligin biosynthesis and processing as a common cause for this brain disorder.
About this Structure
3B3Q is a Protein complex structure of sequences from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA.
Reference
Structural basis for synaptic adhesion mediated by neuroligin-neurexin interactions., Chen X, Liu H, Shim AH, Focia PJ, He X, Nat Struct Mol Biol. 2008 Jan;15(1):50-6. Epub 2007 Dec 16. PMID:18084303
Page seeded by OCA on Thu Mar 20 18:55:51 2008
Categories: Homo sapiens | Mus musculus | Protein complex | Chen, X. | Focia, P. | He, X. | Liu, H. | Shim, A. | CA | NAG | Adhesion | Alternative splicing | Calcium binding | Cell adhesion | Heterophilic | Membrane | Protein-protein complex | Synaptic formation | Transmembrane
