Sandbox Reserved 200: Difference between revisions
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=Introduction= | =Introduction= | ||
[[Image:2D_RNase_A.png|200px|left|thumb|RNase A minor dimer,[[1A2W]]]] | [[Image:2D_RNase_A.png|200px|left|thumb|RNase A minor dimer,[[1A2W]]]] | ||
Bovine pancreatic ribonuclease A [http://en.wikipedia.org/wiki/Ribonuclease_A (RNase A)] is an enzyme that catalyzes the hydrolysis of RNA through [http://www.proteopedia.org/wiki/index.php/Sandbox_Reserved_193 acid-base catalysis]. RNase A has the capability to structurally form dimers, trimers, and other oligomers based on the structure of the [http://www.proteopedia.org/wiki/index.php/Sandbox_Reserved_192 Structure of RNase A monomer]. Unlike the monomers, these oligomers are capable of catalyzing the hydrolysis of double stranded RNA (dsRNA).<ref name=" | Bovine pancreatic ribonuclease A [http://en.wikipedia.org/wiki/Ribonuclease_A (RNase A)] is an enzyme that catalyzes the hydrolysis of RNA through [http://www.proteopedia.org/wiki/index.php/Sandbox_Reserved_193 acid-base catalysis]. RNase A has the capability to structurally form dimers, trimers, and other oligomers based on the structure of the [http://www.proteopedia.org/wiki/index.php/Sandbox_Reserved_192 Structure of RNase A monomer]. Unlike the monomers, these oligomers are capable of catalyzing the hydrolysis of double stranded RNA (dsRNA).<ref name="tumor">PMID:12697760</ref> The oligomers are formed by 3D domain swapping, which can occur once or twice per monomeric unit <ref name="liul">PMID:11224563</ref >. The 3D domain swapping has no impact on the formation of active sites. These same active sites, which are composed of His 12, Lys 41, and His 119, can be found in the monomer, dimer, and trimer <ref name="liul"/>. The oligomers of RNase A also show medical relevance when looking at antitumor drugs as well as the possible cause of Alzheimer's. | ||
=Dimers= | =Dimers= | ||
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The RNase A 3D swapped oligomers show significant biological activity including allostery, antitumor, and immunorepression activity. This same activity has not observed in the monomer and the non-3D domain swapped dimers .<ref name="liu98">PMID:9502384</ref > This could be due to the fact that the monomer has a cystolic RNase A inhibitor that is unable to inhibit the active sites of the oligomers. <ref name="liu01">PMID:11790847</ref > | The RNase A 3D swapped oligomers show significant biological activity including allostery, antitumor, and immunorepression activity. This same activity has not observed in the monomer and the non-3D domain swapped dimers .<ref name="liu98">PMID:9502384</ref > This could be due to the fact that the monomer has a cystolic RNase A inhibitor that is unable to inhibit the active sites of the oligomers. <ref name="liu01">PMID:11790847</ref > | ||
The RNase A 3D domain swapped oligomers show significant biological activity including allostery, antitumor, and immunorepression activity. This same activity has not observed in the monomer and the non-3D domain swapped oligomers .<ref name="liu98">PMID:9502384</ref > This could be due to the fact that the monomer has a cystolic RNase A inhibitor that is unable to inhibit the active sites of the oligomers. <ref name="liu01">PMID:11790847</ref > | |||
All oligomers of RNase A have antitumor activity, but the larger oligomers show greater activity. <ref name="tumor"/> | |||
=Literature Cited= | =Literature Cited= | ||
