Sandbox Reserved 200: Difference between revisions
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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. | 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. | ||
= | =Dimers= | ||
<Structure load='1A2W' size='400' frame='true' align='right' caption='Ribonuclease A Dimer' scene='Sandbox_Reserved_200/Minor_dimer/2' /> | <Structure load='1A2W' size='400' frame='true' align='right' caption='Ribonuclease A Dimer' scene='Sandbox_Reserved_200/Minor_dimer/2' /> | ||
Ribonuclease A has both a major and <scene name='Sandbox_Reserved_200/Minor_dimer/2'>Minor dimer</scene> which are very similar to one another. Though they are similar, they are formed by different types of 3D domain swapping. 3D domain swapping occurs when identical domains are interchanged. The <scene name='Sandbox_Reserved_200/Major_dimer/11'>Major dimer</scene> is formed by 3D domain swapping the β-strand of the C-terminus.<ref name="liu98"/> The minor dimer, on the other hand, is formed by 3D domain swapping its α-helix of the N-terminus <ref name="liu98"/>. Domain swapping is extremely specific and can only occur at the C or N terminus. | |||
The two domains of the dimer are linked via the hinge loop.<ref name="liul"/>. In the major dimer, the hinge loop is composed of residues 112-115. In the minor dimer, the hinge loop is composed of residues 16-22.<ref name="liul"/> The most important component of the hinge loops is Ala19. <scene name='Sandbox_Reserved_200/Minor_dimer_hinge/1'>Ala19</scene> is the reason that the hinge loops are so flexible . This flexibility allows the dimers to adopt different orientations, for example the major and minor structures.<ref name="liu98"/> | |||
<scene name='Sandbox_Reserved_200/Major_dimer/9'>N-terminus</scene> | <scene name='Sandbox_Reserved_200/Major_dimer/9'>N-terminus</scene> | ||
