Sandbox GGC12: Difference between revisions
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The structural highlights of this protein are four: the three domains that compose the protein, the binding site in domain II for salicylates, sulfonamides and several drug ingredients, the bilirubin binding site at position 264, and the free cysteine in the structure of the protein <ref> PMID: 32162429</ref>. | The structural highlights of this protein are four: the three domains that compose the protein, the binding site in domain II for salicylates, sulfonamides and several drug ingredients, the bilirubin binding site at position 264, and the free cysteine in the structure of the protein <ref> PMID: 32162429</ref>. | ||
This is the structural view of <scene name='78/781196/3domains/1'>the three domains</scene> by different colors. Digitoxin, cardiac glycoside, could bind domain I for cardiac insufficiency, warfarin, anticouagulant, bind primarily in domain II, and the diazapines like benzodiazapine, muscular relaxor, in domain III. The shared binding site in domain II between zinc and calcium at residue <scene name='78/781196/273_asp/2'>Asp 273</scene> suggests a crosstalk between zinc and calcium transport in the blood. The <scene name='78/781196/264_bili/1'>bilirubin</scene> binding site at position 264, which is significant because it possess important functions as an antioxidant, but it also serves simply as a means to excrete unwanted heme, derived from various heme-containing proteins such as hemoglobin, myoglobin, and various P450 enzymes. <scene name='78/781196/Cys34/1'>Cys 34</scene> located in a loop between helice is the only cysteine residue that does not participate in any disulfide bridges. Its sulfhydryl group is prevented from coupling with the external counterparts giving a structure known as triclinic crystals. Sequence 143 through 155 and sequence 244 through 263 are involved in ligand binding. For example, residues <scene name='78/781196/Sequence/1'>143-155</scene>, an aromatic sequence, | This is the structural view of <scene name='78/781196/3domains/1'>the three domains</scene> by different colors. Digitoxin, cardiac glycoside, could bind domain I for cardiac insufficiency, warfarin, anticouagulant, bind primarily in domain II, and the diazapines like benzodiazapine, muscular relaxor, in domain III. The shared binding site in domain II between zinc and calcium at residue <scene name='78/781196/273_asp/2'>Asp 273</scene> suggests a crosstalk between zinc and calcium transport in the blood. The <scene name='78/781196/264_bili/1'>bilirubin</scene> binding site at position 264, which is significant because it possess important functions as an antioxidant, but it also serves simply as a means to excrete unwanted heme, derived from various heme-containing proteins such as hemoglobin, myoglobin, and various P450 enzymes. <scene name='78/781196/Cys34/1'>Cys 34</scene> located in a loop between helice is the only cysteine residue that does not participate in any disulfide bridges. Its sulfhydryl group is prevented from coupling with the external counterparts giving a structure known as triclinic crystals. Sequence 143 through 155 and sequence 244 through 263 are involved in ligand binding. For example, residues <scene name='78/781196/Sequence/1'>143-155</scene>, an aromatic sequence, corresponds with the region of the second major long-chain fatty acid binding site <ref>PMID: 2155760</ref>. | ||
corresponds with the region of the second major long-chain fatty acid binding site. | |||
</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
<references/> | <references/> | ||