3b3q: Difference between revisions

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==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.

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==

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[[Category: transmembrane]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:03:04 2008''

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@@ Line 4: / Line 4: @@
 ==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.
+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==
@@ Line 31: / Line 31: @@
 [[Category: transmembrane]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 11:10:56 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:03:04 2008''