3b3q
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 3b3q |SIZE=350|CAPTION= <scene name='initialview01'>3b3q</scene>, resolution 2.4Å | |PDB= 3b3q |SIZE=350|CAPTION= <scene name='initialview01'>3b3q</scene>, resolution 2.4Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> |
|ACTIVITY= | |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]) | |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]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3b3q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b3q OCA], [http://www.ebi.ac.uk/pdbsum/3b3q PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3b3q RCSB]</span> | ||
}} | }} | ||
| Line 28: | Line 31: | ||
[[Category: Liu, H.]] | [[Category: Liu, H.]] | ||
[[Category: Shim, A.]] | [[Category: Shim, A.]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: NAG]] | ||
[[Category: adhesion]] | [[Category: adhesion]] | ||
[[Category: alternative splicing]] | [[Category: alternative splicing]] | ||
| Line 40: | Line 41: | ||
[[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 05:22:44 2008'' |
Revision as of 02:22, 31 March 2008
| |||||||
| , resolution 2.4Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | Nlgn1 (Mus musculus), NRXN1 (Homo sapiens) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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 Mon Mar 31 05:22:44 2008
