Sandbox Reserved 1093: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 52: | Line 52: | ||
'''Ligands''' | '''Ligands''' | ||
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. | 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. | 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. | ||
The structure of the complex <scene name='82/829346/Complex/1'>Nrxn1β–LRRTM2</scene>[http://proteopedia.org/wiki/index.php/5z8y]is being determined by co-crystallisation. A mutation from His 355 to Ala 355 without affecting the complex structure is necessary to maintain the stability of the crystal. | The structure of the complex <scene name='82/829346/Complex/1'>Nrxn1β–LRRTM2</scene>[http://proteopedia.org/wiki/index.php/5z8y]is being determined by co-crystallisation. A mutation from His 355 to Ala 355 without affecting the complex structure is necessary to maintain the stability of the crystal. | ||
PSD-95 [http://proteopedia.org/wiki/index.php/1tq3] is a post synaptic scaffolding protein playing a role in the regulation of the expression of the genes coding for AMPA receptors. This protein also play a role in the translocation of LRRTM2 after the translation. | |||
