Sandbox Reserved 200: Difference between revisions
Lexi Gehring (talk | contribs) No edit summary |
Lexi Gehring (talk | contribs) No edit summary |
||
| Line 5: | Line 5: | ||
=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]. 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"/>. | 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]. 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. | ||
=Minor Dimer= | =Minor Dimer= | ||
<Structure load='1A2W' size='400' frame='true' align='right' caption='Ribonuclease A Dimer' scene='Sandbox_Reserved_200/Minor_dimer/2' /> | |||
<scene name='Sandbox_Reserved_200/Minor_dimer_hinge/1'>Ala19</scene> | <scene name='Sandbox_Reserved_200/Minor_dimer_hinge/1'>Ala19</scene> | ||
Revision as of 06:49, 31 March 2011
| This Sandbox is Reserved from Feb 02, 2011, through Jul 31, 2011 for use by the Biochemistry II class at the Butler University at Indianapolis, IN USA taught by R. Jeremy Johnson. This reservation includes Sandbox Reserved 191 through Sandbox Reserved 200. |
To get started:
More help: Help:Editing |
IntroductionIntroduction
Bovine pancreatic ribonuclease A (RNase A) is an enzyme that catalyzes the hydrolysis of RNA through acid-base catalysis. RNase A has the capability to structurally form dimers, trimers, and other oligomers based on the structure of the Structure of RNase A monomer. The oligomers are formed by 3D domain swapping, which can occur once or twice per monomeric unit [1]. 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 [1]. The oligomers of RNase A also show medical relevance when looking at antitumor drugs as well as the possible cause of Alzheimer's.
Minor DimerMinor Dimer
|
Major DimerMajor Dimer
TrimersTrimers
|
Medical RelevanceMedical Relevance
The RNase A 3D swapped dimers show significant biological activity. This biological activity includes allostery, antitumor and immunorepression activity. This same activity was not observed in the monomer and the non-3D domain swapped dimers .[2] This could be due to the fact that the monomer has a cystolic RNase A inhibitor. [3]
Literature CitedLiterature Cited
- ↑ 1.0 1.1 Liu Y, Gotte G, Libonati M, Eisenberg D. A domain-swapped RNase A dimer with implications for amyloid formation. Nat Struct Biol. 2001 Mar;8(3):211-4. PMID:11224563 doi:10.1038/84941
- ↑ Clemo FA. Urinary enzyme evaluation of nephrotoxicity in the dog. Toxicol Pathol. 1998 Jan-Feb;26(1):29-32. PMID:9502384
- ↑ Liu Y, Gotte G, Libonati M, Eisenberg D. Structures of the two 3D domain-swapped RNase A trimers. Protein Sci. 2002 Feb;11(2):371-80. PMID:11790847