Sandbox 215: Difference between revisions

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CETP's structure can be divided into four structural units:

* At each end of the protein there is a barrel which is constitued of highly twisted ß-sheet and two helices called A and B at the N-terminal and A', B' at C-terminal extremity. Helices B and B' are longer than A and A'

* At each end of the protein there is a barrel which is constitued of highly twisted β-sheet and two helices called A and B at the N-terminal and A', B' at C-terminal extremity. Helices B and B' are longer than A and A'

* Between the two barrels there is a central ß-sheet which is constitued of six antiparallel strands

* Between the two barrels there is a central β-sheet which is constitued of six antiparallel strands

* At the C-terminal extremity there is a distorted amphiphathic helix called helix X which is an extension of C-teminal interacting with N-terminal residues.

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CETP's structure reveals a 60 Å long hydrophobic tunnel which traverses the core of the molecule and contains four lipid binding sites: two neutral lipids binding sites in the middle of the tunnel and two phospholipids binding sites (one at each end). The center of the tunnel which is called the “neck” is 10 Å wide and 5 Å high that is large enough to permit the passage of neutral lipid.

A wall of ß-sheets underneath the lipids and a layer of helices above the lipids forms the longest tunnel that it exists in lipid-binding and lipid-transfer protein.

A wall of β-sheets underneath the lipids and a layer of helices above the lipids forms the longest tunnel that it exists in lipid-binding and lipid-transfer protein.

Cholesteryl ester 1 (CE1) is situated between the N barrel and the central ß-sheet. This binding site is mostly composed of hydrophobic residues and only a few polar. CE1 is too far away from the Ser 230 to establish a hydrogen bond but CE1 can establish some π-starking interaction.

Cholesteryl ester 1 (CE1) is situated between the N barrel and the central β-sheet. This binding site is mostly composed of hydrophobic residues and only a few polar. CE1 is too far away from the Ser 230 to establish a hydrogen bond but CE1 can establish some π-starking interaction.

Cholesteryl ester 2 penetrates deeper into the barrel than CE1 and resides between the central ß-sheet and the C-barrel. 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.

Cholesteryl ester 2 penetrates deeper into the barrel than CE1 and resides between the central β-sheet and the C-barrel. 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.

The N-opening of the tunnel is 10 Å wide and 5 Å high whereas the C-opening is 13 Å X 5 Å. The C-opening is a little bit larger but both are large enough to allow lipid access.

Sandbox 215: Difference between revisions

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@@ Line 18: / Line 18: @@
 CETP's structure can be divided into four structural units:
-* At each end of the protein there is a barrel which is constitued of highly twisted ß-sheet and two helices called A and B at the N-terminal and A', B' at C-terminal extremity. Helices B and B' are longer than A and A'
+* At each end of the protein there is a barrel which is constitued of highly twisted β-sheet and two helices called A and B at the N-terminal and A', B' at C-terminal extremity. Helices B and B' are longer than A and A'
-* Between the two barrels there is a central ß-sheet which is constitued of six antiparallel strands
+* Between the two barrels there is a central β-sheet which is constitued of six antiparallel strands
 * At the C-terminal extremity there is a distorted amphiphathic helix called helix X which is an extension of C-teminal interacting with N-terminal residues.
@@ Line 26: / Line 26: @@
 CETP's structure reveals a 60 Å long hydrophobic tunnel which traverses the core of the molecule and contains four lipid binding sites: two neutral lipids binding sites in the middle of the tunnel and two phospholipids binding sites (one at each end). The center of the tunnel which is called the “neck” is 10 Å wide and 5 Å high that is large enough to permit the passage of neutral lipid.
-A wall of ß-sheets underneath the lipids and a layer of helices above the lipids forms the longest tunnel that it exists in lipid-binding and lipid-transfer protein.
+A wall of β-sheets underneath the lipids and a layer of helices above the lipids forms the longest tunnel that it exists in lipid-binding and lipid-transfer protein.
-Cholesteryl ester 1 (CE1) is situated between the N barrel and the central ß-sheet. This binding site is mostly composed of hydrophobic residues and only a few polar. CE1 is too far away from the Ser 230 to establish a hydrogen bond but CE1 can establish some π-starking interaction.
+Cholesteryl ester 1 (CE1) is situated between the N barrel and the central β-sheet. This binding site is mostly composed of hydrophobic residues and only a few polar. CE1 is too far away from the Ser 230 to establish a hydrogen bond but CE1 can establish some π-starking interaction.
-Cholesteryl ester 2 penetrates deeper into the barrel than CE1 and resides between the central ß-sheet and the C-barrel. 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.
+Cholesteryl ester 2 penetrates deeper into the barrel than CE1 and resides between the central β-sheet and the C-barrel. 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.
 The N-opening of the tunnel is 10 Å wide and 5 Å high whereas the C-opening is 13 Å X 5 Å. The C-opening is a little bit larger but both are large enough to allow lipid access.