Sandbox Reserved 346: Difference between revisions
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<scene name='Sandbox_Reserved_346/Ast/1'>AST</scene> is a homodimer that contains 16 alpha helices and a Beta-sheet formed from 7 parallel and antiparallel strands.Each subunit contain an equivalent active site. The subunits connect between their large domains and between the the N-terminal residues and the large domain of the other subunit. This structure of AST varies minutely among organisms rangin from ''E. coli'' to humans. The structure of the active site is highly conserved, and their is a sequence homology of 25%. | <scene name='Sandbox_Reserved_346/Ast/1'>AST</scene> is a homodimer that contains 16 alpha helices and a Beta-sheet formed from 7 parallel and antiparallel strands.Each subunit contain an equivalent active site. The subunits connect between their large domains and between the the N-terminal residues and the large domain of the other subunit. This structure of AST varies minutely among organisms rangin from ''E. coli'' to humans. The structure of the active site is highly conserved, and their is a sequence homology of 25%. | ||
Each subunit of the homo dimer is further divided into a samll and large domain. The | Each subunit of the homo dimer is further divided into a samll and large domain. The <scene name='Sandbox_Reserved_346/Small_subunit/1'>smal domain</scene> is comprises of the amino acids from the N-terminus to the Pro 48 residue and from the Met 326 residue to the C-terminus. The remaining amino acids make up the large domain, and the two domains are connected by a long alpha helicx consisting of 32 amino acids. | ||
The large domain is where the active site of AST is found and to accomadate this the core is contains many alpha/beta supersecondary structures. This is contrasted with the core of the small subunit which is fromed from two alpha hellices and two beta strands. In multicellular organisms there is a kink at the 325th residue which acts as a hinge for the samll domain, which allows for the resulting conformational changes that take place upon the binding of inhibitors to the enzyme. | The large domain is where the active site of AST is found and to accomadate this the core is contains many alpha/beta supersecondary structures. This is contrasted with the core of the small subunit which is fromed from two alpha hellices and two beta strands. In multicellular organisms there is a kink at the 325th residue which acts as a hinge for the samll domain, which allows for the resulting conformational changes that take place upon the binding of inhibitors to the enzyme. | ||