Sandbox Reserved 1093: Difference between revisions

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'''Other synaptic organisers'''

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Neuroligins (NLs)

LRRTM2 bind to Neurexins 1, 2 and 3 ︎and ︎a variant region at splice site 4 in the LNS. As the variant region lacking a 30 amino acid insert (-S4), LRRTM2 cannot induce presynaptic differentiation in neurons. On the contrary, Neuroligin1 binds to Neurexins 1, 2, and 3 ︎ but not ︎to variants, has a higher affinity with Neurexin 1 (-S4) than with Neurexin 1 (+S4)

~~Cbln1–GluD2~~

LRRTM2 bind to Neurexins 1, 2 and 3 ︎and ︎a variant region at splice site 4 in the LNS. As the variant region lacking a 30 amino acid insert (-S4), LRRTM2 cannot induce presynaptic differentiation in neurons. On the contrary, Neuroligin1 binds to Neurexins 1, 2, and 3, has a higher affinity with Neurexin 1 (-S4) than with Neurexin 1 (+S4)

GluD2[[http://proteopedia.org/wiki/index.php/5cc2]]

'''Neurexins'''

Neurexins (Nrxns) [http://proteopedia.org/wiki/index.php/Neurexin]is a family of presynaptic organizer which interact with several postsynaptic organizers such as LRRTM2.

Neurexins (Nrxns) [http://proteopedia.org/wiki/index.php/Neurexin]is a family of the presynaptic organizer which interact with several postsynaptic organizers such as LRRTM2.

There are three Neurexin genes in vertebrates, each corresponding to a different promoter type. Neurexins are characterized by their laminin-neurexin-sex hormone (LNS) domains. ︎ <scene name='82/829346/Neurexin_1_alpha/1'>α-neurexins</scene> have six whereas ︎<scene name='82/829346/Beta-neurexin_1/2'>β-neurexins</scene> have a single LNS domain. The α-helical conformation causes severe steric hindrance with the bound LRRTM2, whereas the β-stranded conformation causes no obvious steric hindrance.

Sandbox Reserved 1093: Difference between revisions

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@@ Line 42: / Line 42: @@
 '''Other synaptic organisers'''
-�
 Neuroligins (NLs)
-LRRTM2 bind to Neurexins 1, 2 and 3 ︎and ︎a variant region at splice site 4 in the LNS. As the variant region lacking a 30 amino acid insert (-S4), LRRTM2 cannot induce presynaptic differentiation in neurons. On the contrary, Neuroligin1 binds to Neurexins 1, 2, and 3 ︎ but not ︎to variants, has a higher affinity with Neurexin 1 (-S4) than with Neurexin 1 (+S4)
-Cbln1–GluD2
+LRRTM2 bind to Neurexins 1, 2 and 3 ︎and ︎a variant region at splice site 4 in the LNS. As the variant region lacking a 30 amino acid insert (-S4), LRRTM2 cannot induce presynaptic differentiation in neurons. On the contrary, Neuroligin1 binds to Neurexins 1, 2, and 3, has a higher affinity with Neurexin 1 (-S4) than with Neurexin 1 (+S4)
+GluD2[[http://proteopedia.org/wiki/index.php/5cc2]]
 '''Neurexins'''
-Neurexins (Nrxns) [http://proteopedia.org/wiki/index.php/Neurexin]is a family of presynaptic organizer  which interact with several postsynaptic organizers such as LRRTM2.
+Neurexins (Nrxns) [http://proteopedia.org/wiki/index.php/Neurexin]is a family of the presynaptic organizer which interact with several postsynaptic organizers such as LRRTM2.
 There are three Neurexin genes in vertebrates, each corresponding to a different promoter type. Neurexins are characterized by their laminin-neurexin-sex hormone (LNS) domains. ︎ <scene name='82/829346/Neurexin_1_alpha/1'>α-neurexins</scene> have six whereas ︎<scene name='82/829346/Beta-neurexin_1/2'>β-neurexins</scene> have a single LNS domain. The α-helical conformation causes severe steric hindrance with the bound LRRTM2, whereas the β-stranded conformation causes no obvious steric hindrance.