Sandbox 215: Difference between revisions

Line 36:

*Cholesteryl ester 2 (CE2) is situated between the central β-sheet and the C-barrel. CE2 penetrates deeper into the barrel than CE1. This site contains even fewer polar groups than CE1 binding site. That's why CE2 is not able to make any hydrogen-bonding or π-starking interaction.

=== Helix X and Ω flaps===

=== Mobile structures: Helix X and Ω flaps===

Some mobile structures located near tunnel openings can facilitate the lipid transfer.

The <scene name='Sandbox_215/Helix_x/1'>helix X</scene> belongs to the C-terminal domain ~~and~~ thanks to ~~its~~

The amphiphathic <scene name='Sandbox_215/Helix_x/1'>helix X</scene> which belongs to the C-terminal domain is flexible thanks to her

<scene name='Sandbox_215/Gly462-phe463-pro464/1'>Gly462-Phe463-Pro464</scene>groupment ~~is flexible. It is an amphiphathic helix~~. The hydrophobic face of helix X interacts with phosphatidylcholine 1 located at the N-terminal in order to form an apolar path allowing the access of neutral lipids to the tunnel. Mutations on the hydrophobic face of helix X reduce transfer activities whereas mutations on the polar side do not have any effects on transfer activities. These results prove that helix X plays an important role in transferring neutral lipid ~~from lipoprotein to CETP~~.

<scene name='Sandbox_215/Gly462-phe463-pro464/1'>Gly462-Phe463-Pro464</scene> groupment. The hydrophobic face of helix X interacts with phosphatidylcholine 1 located at the N-terminal in order to form an apolar path allowing the access of neutral lipids to the tunnel. Mutations on the hydrophobic face of helix X reduce transfer activities whereas mutations on the polar side do not have any effects on transfer activities. These results prove that helix X plays an important role in transferring neutral lipid between lipoproteins.

Near the C-opening, there are also two Ω flaps: Ω1 and Ω2. These flaps are linked through ~~the~~ starking interaction between the Phe292 and Ph350. The flap Ω1 interacts with the oleoyl tail of the cholesteryl ester 2 in order to protect the lipid from aqueous solvent exposure~~. Ω1 flap~~ also ~~helps~~ the exchange of lipids through the C opening.

Near the C-opening, there are also two Ω flaps: Ω1 and Ω2. These flaps are linked through a starking interaction between the Phe292 and Ph350. The flap Ω1 interacts with the oleoyl tail of the cholesteryl ester 2 in order to protect the lipid from aqueous solvent exposure and also to help the exchange of lipids through the C opening.

== Mechanism allowing neutral-lipid and phospholipid transfer ==

Sandbox 215: Difference between revisions

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@@ Line 36: / Line 36: @@
 *Cholesteryl ester 2 (CE2) is situated between the central β-sheet and the C-barrel. CE2 penetrates deeper into the barrel than CE1. This site contains even fewer polar groups than CE1 binding site. That's why CE2 is not able to make any hydrogen-bonding or π-starking interaction.
-=== Helix X and Ω flaps===
+=== Mobile structures: Helix X and Ω flaps===
 Some mobile structures located near tunnel openings can facilitate the lipid transfer.
-The <scene name='Sandbox_215/Helix_x/1'>helix X</scene> belongs to the C-terminal domain and thanks to its
+The amphiphathic <scene name='Sandbox_215/Helix_x/1'>helix X</scene> which belongs to the C-terminal domain is  flexible thanks to her
-<scene name='Sandbox_215/Gly462-phe463-pro464/1'>Gly462-Phe463-Pro464</scene>groupment is flexible. It is an amphiphathic helix. The hydrophobic face of helix X interacts with phosphatidylcholine 1 located at the N-terminal in order to form an apolar path allowing the access of neutral lipids to the tunnel. Mutations on the hydrophobic face of helix X reduce transfer activities whereas mutations on the polar side do not have any effects on transfer activities. These results prove that helix X plays an important role in transferring neutral lipid from lipoprotein to CETP.
+<scene name='Sandbox_215/Gly462-phe463-pro464/1'>Gly462-Phe463-Pro464</scene> groupment. The hydrophobic face of helix X interacts with phosphatidylcholine 1 located at the N-terminal in order to form an apolar path allowing the access of neutral lipids to the tunnel. Mutations on the hydrophobic face of helix X reduce transfer activities whereas mutations on the polar side do not have any effects on transfer activities. These results prove that helix X plays an important role in transferring neutral lipid between lipoproteins.
-Near the C-opening, there are also two Ω flaps:  Ω1 and  Ω2. These flaps are linked through the starking interaction between the Phe292 and Ph350. The flap Ω1 interacts with the oleoyl tail of the cholesteryl ester 2 in order to protect the lipid from aqueous solvent exposure. Ω1 flap also helps the exchange of lipids through the C opening.
+Near the C-opening, there are also two Ω flaps: Ω1 and Ω2. These flaps are linked through a starking interaction between the Phe292 and Ph350. The flap Ω1 interacts with the oleoyl tail of the cholesteryl ester 2 in order to protect the lipid from aqueous solvent exposure and also to help the exchange of lipids through the C opening.
 == Mechanism allowing neutral-lipid and phospholipid transfer ==