3b3q

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[[Image:3b3q.jpg|left|200px]]
[[Image:3b3q.jpg|left|200px]]
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{{Structure
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|PDB= 3b3q |SIZE=350|CAPTION= <scene name='initialview01'>3b3q</scene>, resolution 2.4&Aring;
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The line below this paragraph, containing "STRUCTURE_3b3q", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>
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|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])
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|DOMAIN=
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{{STRUCTURE_3b3q| PDB=3b3q | SCENE= }}
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|RELATEDENTRY=
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|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>
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'''Crystal structure of a synaptic adhesion complex'''
'''Crystal structure of a synaptic adhesion complex'''
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[[Category: Liu, H.]]
[[Category: Liu, H.]]
[[Category: Shim, A.]]
[[Category: Shim, A.]]
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[[Category: adhesion]]
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[[Category: Adhesion]]
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[[Category: alternative splicing]]
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[[Category: Alternative splicing]]
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[[Category: calcium binding]]
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[[Category: Calcium binding]]
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[[Category: cell adhesion]]
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[[Category: Cell adhesion]]
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[[Category: heterophilic]]
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[[Category: Heterophilic]]
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[[Category: membrane]]
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[[Category: Membrane]]
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[[Category: protein-protein complex]]
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[[Category: Protein-protein complex]]
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[[Category: synaptic formation]]
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[[Category: Synaptic formation]]
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[[Category: transmembrane]]
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[[Category: Transmembrane]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 20:21:40 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:22:44 2008''
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Revision as of 17:21, 4 May 2008

Template:STRUCTURE 3b3q

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 Sun May 4 20:21:40 2008

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