Sandbox 215: Difference between revisions
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==Structure== | ==Your Heading Here (maybe something like 'Structure')==<StructureSection load='1dq8' size='500' side='right' caption='Structure of HMG-CoA reductase (PDB entry [[1dq8]])' scene=''>==Structure== | ||
<Structure load='2obd' size='400' frame='true' align='left' caption='Structure of cholesteryl ester transfer protein' scene='Insert optional scene name here' (PDB entry [[2obd]])'/>2OBD is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo Sapiens]. Full crystallographic information is available from [http://www.ebi.ac.uk/msd-srv/oca/oca-bin/ocashort?id=2OBD OCA] | <Structure load='2obd' size='400' frame='true' align='left' caption='Structure of cholesteryl ester transfer protein' scene='Insert optional scene name here' (PDB entry [[2obd]])'/> | ||
2OBD is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo Sapiens]. Full crystallographic information is available from [http://www.ebi.ac.uk/msd-srv/oca/oca-bin/ocashort?id=2OBD OCA] | |||
===Overview of the structure=== | ===Overview of the structure=== | ||
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The amphiphathic <scene name='Sandbox_215/Helix_x/1'>helix X</scene> which belongs to the C-terminal domain is flexible thanks to her | 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. 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. | <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 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. | 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.</StructureSection> | ||
== Mechanism allowing neutral-lipid and phospholipid transfer == | == Mechanism allowing neutral-lipid and phospholipid transfer == | ||
