Sandbox Reserved 1456: Difference between revisions
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The mechanism of action of Kgp is largely determined by its <scene name='79/799584/Active_site_2/1'>active site</scene>. By binding the ligand to the active site, Kgp is now capable of performing its virulytic activities. The temporary stability of the ligand by the amino acids in the active site allows Kgp to be specific in its activity and achieve optimal function. | The mechanism of action of Kgp is largely determined by its <scene name='79/799584/Active_site_2/1'>active site</scene>. By binding the ligand to the active site, Kgp is now capable of performing its virulytic activities. The temporary stability of the ligand by the amino acids in the active site allows Kgp to be specific in its activity and achieve optimal function. | ||
There are many other features of the protein that contribute to its overall structure and function. | There are many other features of the protein that contribute to its overall structure and function. As mentioned previously, Kgp also has two fundamental components, a catalytic domain and an immunoglobulin-superfamily domain. These two aid in the catalytic function of the protein and are connected at Pro600 of CD and Lys601 of IgSF <ref>PMID: 15554977</ref>. Lys601 allows the polypeptide chain to enter the IgSF, essential for folding of Kgp. Without this connection at Lys601, Kgp-specific activity would not be possible since proper binding of Kgp and IgSF is absent. In the active site of Kgp, the catalytic triad is formed with Cys477-His444-Asp388. Aspartate in position 388 is favored over glutamate: with glutamate protruding slightly more than aspartate, the lysine ligand (CKC) is able to get closer to the catalytic His444, thus allowing the protein to function that much more efficiently <ref>PMID: 23776206</ref>. | ||
</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
<references/> | <references/> | ||