Sandbox Reserved 200: Difference between revisions
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Not only is the structure of the monomers conserved in the dimers, but the active is also conserved. <ref name="liu98"/> The active site of both dimers contains His12, Lys41, and His119 residues. The active sites are a composite of the monomer subunits containing His12 from one monomer and His119 form the other monomer.<ref name="liul"/> During domain swapping, the active site is not disturbed, so the dimers are able to retain their enzymatic activity. | Not only is the structure of the monomers conserved in the dimers, but the active is also conserved. <ref name="liu98"/> The active site of both dimers contains His12, Lys41, and His119 residues. The active sites are a composite of the monomer subunits containing His12 from one monomer and His119 form the other monomer.<ref name="liul"/> During domain swapping, the active site is not disturbed, so the dimers are able to retain their enzymatic activity. | ||
==Trimers== | ==Trimers== | ||
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Similar to dimer, the structure of the monomer is conserved except for the <scene name='Sandbox_Reserved_200/Minor_trimer/2'>hinge loop</scene>. The <scene name='Sandbox_Reserved_200/Minor_trimer/3'>active sites</scene> of the trimers are made up of the same amino acid residues as the monomers and dimers. The trimer's active site is slightly different from that of the monomer and dimer because it has a sulfate ion trap.<ref name="liu01"/> A total of four sulfate ions bind to the minor trimer, three to the active sites, and one to the hinge loop. <scene name='Sandbox_Reserved_200/Minor_trimer/5'>Gly112</scene> residues from each subunit as well as other amino acid residues bind to the sulfate ion. An intricate network of hydrogen bonding holds the sulfate ion in the trap. <ref name="liu01"/> The monomers and dimers also have sulfate ions bond to their active site, but the ions seem to have a stronger presence within the trimer. The ions are bound to the active site are completely surrounded by water which is responsible for the <scene name='Sandbox_Reserved_200/Minor_trimer/7'>hydrogen bonding</scene> to the sulfate ion. | Similar to dimer, the structure of the monomer is conserved except for the <scene name='Sandbox_Reserved_200/Minor_trimer/2'>hinge loop</scene>. The <scene name='Sandbox_Reserved_200/Minor_trimer/3'>active sites</scene> of the trimers are made up of the same amino acid residues as the monomers and dimers. The trimer's active site is slightly different from that of the monomer and dimer because it has a sulfate ion trap.<ref name="liu01"/> A total of four sulfate ions bind to the minor trimer, three to the active sites, and one to the hinge loop. <scene name='Sandbox_Reserved_200/Minor_trimer/5'>Gly112</scene> residues from each subunit as well as other amino acid residues bind to the sulfate ion. An intricate network of hydrogen bonding holds the sulfate ion in the trap. <ref name="liu01"/> The monomers and dimers also have sulfate ions bond to their active site, but the ions seem to have a stronger presence within the trimer. The ions are bound to the active site are completely surrounded by water which is responsible for the <scene name='Sandbox_Reserved_200/Minor_trimer/7'>hydrogen bonding</scene> to the sulfate ion. | ||
==Enzymatic Activity== | |||
The monomers, dimers, and trimers all have significant enzymatic activity. The higher the order of the oligomer, the better its enzymatic activity is.<ref name="liu01"/> The pentamers, though their structure is not known, have shown the greatest enzymatic activity. Though the high order oligomers are better enzymes, they are also degraded to their subunits faster. The trimer will degrade to a dimer which will eventually degrade to a monomer. | |||
The major dimer is more active than the minor dimer, while the minor trimer is more active than the major trimer.<ref name="liu01"/> It has been shown that the smaller the distance between two active sites, the greater the enzymatic activity on dsRNA. The higher ordered oligomers are typically more tightly packed which would decrease the distance between active sites, and make them more active.<ref name="liu01"/> Liu et. al. also predicts taht teh twisted orientation of the dimers and trimers allows for the destabilization of dsRNA. Because the monomer does not have a twisted structure, it is not able to destabilize dsRNA.<ref name="liu01"/> | |||
==Medical Relevance== | ==Medical Relevance== | ||
