Sandbox Reserved 955: Difference between revisions

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OCA, Jérémy Wagner

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	HIV-1 protease is a dimer of identical polypeptide chains : it's composed of two symmetrically related subunits, each consisting of 99 amino acid residues. Its structure is composed of A,B chains,<scene name='60/604474/Helix/1'>two helix</scene> (one in each subunit)and <scene name='60/604474/Sheets/2'>16 bêta sheets</scene>(8 in each subunits).		HIV-1 protease is a dimer of identical polypeptide chains : it's composed of two symmetrically related subunits, each consisting of 99 amino acid residues. Its structure is composed of A,B chains,<scene name='60/604474/Helix/1'>two helix</scene> (one in each subunit)and <scene name='60/604474/Sheets/2'>16 bêta sheets</scene>(8 in each subunits).

	The active site of the protease is localised inside the tunnel forms by the two subunits of the protein which come together, and it consists of two <scene name='60/604474/Catalytic/5'>Asp-Thr-Gly</scene> conserved sequences, making it the member of the aspartyl protease family.On the top of this tunnel are ~~txo~~ flexible flaps which move to allow proteins to enter the tunnel and thus the catalytic site : they shift from an open to a closed conformation in order to bind the target in a correct conformation for cleavage. The two Asp's are essential catalytic residues either interact with the incoming water or protonate the carbonyl to make the carbon more electrophilic for the incoming water. <ref>http://proteopedia.org/wiki/index.php/HIV-1_protease</ref>		The active site of the protease is localised inside the tunnel forms by the two subunits of the protein which come together, and it consists of two <scene name='60/604474/Catalytic/5'>Asp-Thr-Gly</scene> conserved sequences, making it the member of the aspartyl protease family.On the top of this tunnel are two flexible flaps which move to allow proteins to enter the tunnel and thus the catalytic site : they shift from an open to a closed conformation in order to bind the target in a correct conformation for cleavage. The two Asp's are essential catalytic residues either interact with the incoming water or protonate the carbonyl to make the carbon more electrophilic for the incoming water. <ref>http://proteopedia.org/wiki/index.php/HIV-1_protease</ref>