Human Caspase-1: Difference between revisions
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<StructureSection load='2h4w' size='500' frame='true' align='right' caption='Caspase-1' scene=''> | <StructureSection load='2h4w' size='500' frame='true' align='right' caption='Caspase-1 complex with allosteric ligand [[2h4w]]' scene=''> | ||
==Introduction== | ==Introduction== | ||
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Caspase-1 also displays cooperative binding through active states, an on-state when ligand is bound and an off state when the active site is vacant or when synthetic ligands are bound at the allosteric site. The allosteric site exists at the dimer interface and is connected to the active sites by a system of 21 hydrogen bonds from 9 residues. Of these 9 residues, only two have a major effect on enzyme activity- <scene name='Human_Caspase-1/Allosteric_salt_bridge/1'>Arg286 and Glu390</scene>, which form a salt bridge. Although only some of the residues are necessary for activity, the continuous string of interactions connecting the active site to the allosteric site to the second active site make up a kind of circuit leading to cooperative binding. <ref name=Datta>PMID:18590738</ref> | Caspase-1 also displays cooperative binding through active states, an on-state when ligand is bound and an off state when the active site is vacant or when synthetic ligands are bound at the allosteric site. The allosteric site exists at the dimer interface and is connected to the active sites by a system of 21 hydrogen bonds from 9 residues. Of these 9 residues, only two have a major effect on enzyme activity- <scene name='Human_Caspase-1/Allosteric_salt_bridge/1'>Arg286 and Glu390</scene>, which form a salt bridge. Although only some of the residues are necessary for activity, the continuous string of interactions connecting the active site to the allosteric site to the second active site make up a kind of circuit leading to cooperative binding. <ref name=Datta>PMID:18590738</ref> | ||
==3D structures of caspase== | |||
[[Caspase]] | |||
</StructureSection> | </StructureSection> | ||