Sandbox GGC12: Difference between revisions
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This is the structural view of <scene name='78/781196/3domains/1'>the three domains</scene> by different colors. Warfarin, anticouagulant, is believed to bind primarily in domain II, and the diazapines like benzodiazapine, muscular relaxor, in | This is the structural view of <scene name='78/781196/3domains/1'>the three domains</scene> by different colors. Warfarin, anticouagulant, is believed to 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. | 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. | |||
</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
<references/> | <references/> | ||
