Sandbox Reserved 1093: Difference between revisions
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1) <scene name='82/829346/Lrrtm2/3'>N-term fixation domain</scene> | 1) <scene name='82/829346/Lrrtm2/3'>N-term fixation domain</scene> | ||
The N-terminal signal peptide is long of 33 amino. The extracellular domain contains 399 amino acids organized in 2 cysteine-rich domains (<scene name='82/829346/Lrrnt/1'>LRRNT</scene> and <scene name='82/829346/Lrrct/1'>LRRCT</scene>) and <scene name='82/829346/Lrr/2'>10 leucine rich domains</scene> (LRR). Each LRR domain is composed of 21 amino acids containing the conserved 11-aa sequence, LxxLxLxxN/ CxL, where x is any amino acid, and <scene name='82/829346/ | The N-terminal signal peptide is long of 33 amino. The extracellular domain contains 399 amino acids organized in 2 cysteine-rich domains (<scene name='82/829346/Lrrnt/1'>LRRNT</scene> and <scene name='82/829346/Lrrct/1'>LRRCT</scene>) and <scene name='82/829346/Lrr/2'>10 leucine rich domains</scene> (LRR). Each LRR domain is composed of 21 amino acids containing the conserved 11-aa sequence, LxxLxLxxN/ CxL, where x is any amino acid, and <scene name='82/829346/Leucine/1'>leucine</scene> and asparagine can be replaced with other hydrophobic residues. The leucine rich repeat domain forms a convex structure stabilized by a <scene name='82/829346/Phe/1'>Phe</scene> spine. The concave surface is composed of a continuous <scene name='82/829346/Beta_sheets/1'>β-sheet</scene>, which provides an effective ligand-binding site, whereas the convex surface consists of <scene name='82/829346/Alpha_helix/1'>α-helices</scene>, which affect the curvature of the LRR domain. | ||
The N-terminal domain allows for the fixation of neurexins (Nrxns) [http://proteopedia.org/wiki/index.php/Neurexin] which bind to the concave surface of the LRR1-LRR5 part of the protein. This fixation is mediated by calcium ions which interacts with the Asp144 and Asp212 of LRRTMT2. It was also observed that LRRTM2 Glu348 interacts with Ca2+ through a water molecule. In top of the Ca2+ mediated interaction, there is the formation of a hydrogen bound between the Asp352 of LRRTM2 and the Arg206 of Nrxns as well as hydrophobic interactions between the LRRTM2 Phe357 and Nrxns Leu208. | The N-terminal domain allows for the fixation of neurexins (Nrxns) [http://proteopedia.org/wiki/index.php/Neurexin] which bind to the concave surface of the LRR1-LRR5 part of the protein. This fixation is mediated by calcium ions which interacts with the Asp144 and Asp212 of LRRTMT2. It was also observed that LRRTM2 Glu348 interacts with Ca2+ through a water molecule. In top of the Ca2+ mediated interaction, there is the formation of a hydrogen bound between the Asp352 of LRRTM2 and the Arg206 of Nrxns as well as hydrophobic interactions between the LRRTM2 Phe357 and Nrxns Leu208. | ||
The fixation of Nrxns doesn’t change the conformation of the protein aside from Glu348 flipping toward the calcium ions. | The fixation of Nrxns doesn’t change the conformation of the protein aside from Glu348 flipping toward the calcium ions. | ||
