Sandbox Reserved 960: Difference between revisions

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=== Cavity ===

The dynamic structure of the protein is responsible of the ligand’s binding by adjustement of position. The structure looses its flexibility when <scene name='60/604479/Cmj/3'>CMJ</scene> binds. The successful delivery of the effector to the receptor relies on this property. The ligand ~~accepting entry of the~~ cavity is formed by H2, H4 and H5 (scene). ~~However, the inside~~ of the cavity is ~~formed by the loop between helixes H3 and H4,~~ and the ~~region from H4 to H5(scene)~~. The cavity is prone to accept such ligand because of its specific composition. Indeed, cavity components are mainly <scene name='60/604479/Hydrophobic_residues/2'>hydrophobic and aromatic</scene> and are localized in the ~~same faces~~ of the helix.Thus, it implies that ~~this~~ residues ~~are regularly distant~~ in the primary structure.

The dynamic structure of the protein is responsible of the ligand’s binding by adjustement of position. The structure looses its flexibility when <scene name='60/604479/Cmj/3'>CMJ</scene> binds. The successful delivery of the effector to the receptor relies on this property. The ligand binding pocket consists in a cavity formed by the helices H2, H4 and H5(scene), arranged in a globular shape.

The top of the cavity is not closed and can establish contacts with the solvent. The cavity is prone to accept such ligand because of its specific composition. Indeed, cavity components are mainly <scene name='60/604479/Hydrophobic_residues/2'>hydrophobic and aromatic</scene>.They consequently interact with the ligand's hydrophobic carbon chain and are localized on the internal face of the helix.Thus, it implies that these residues respect a regular distance pattern in the primary structure of the ASP1.

=== Ligands ===

Sandbox Reserved 960: Difference between revisions

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@@ Line 62: / Line 62: @@
 === Cavity ===
-The dynamic structure of the protein is responsible of the ligand’s binding by adjustement of position. The structure looses its flexibility when <scene name='60/604479/Cmj/3'>CMJ</scene> binds. The successful delivery of the effector to the receptor relies on this property. The ligand accepting entry of the cavity is formed by H2, H4 and H5 (scene). However, the inside of the cavity is formed by the loop between helixes H3 and H4, and the region from H4 to H5(scene). The cavity is prone to accept such ligand because of its specific composition. Indeed, cavity components are mainly  <scene name='60/604479/Hydrophobic_residues/2'>hydrophobic and aromatic</scene> and are localized in the same faces of the helix.Thus, it implies that this residues are regularly distant in the primary structure.
+The dynamic structure of the protein is responsible of the ligand’s binding by adjustement of position. The structure looses its flexibility when <scene name='60/604479/Cmj/3'>CMJ</scene> binds. The successful delivery of the effector to the receptor relies on this property. The ligand binding pocket consists in a cavity formed by the helices H2, H4 and H5(scene), arranged in a globular shape.
+The top of the cavity is not closed and can establish contacts with the solvent. The cavity is prone to accept such ligand because of its specific composition. Indeed, cavity components are mainly <scene name='60/604479/Hydrophobic_residues/2'>hydrophobic and aromatic</scene>.They consequently interact with the ligand's hydrophobic carbon chain and are localized on the internal face of the helix.Thus, it implies that these residues respect a regular distance pattern in the primary structure of the ASP1.
 === Ligands ===