Sandbox GGC15: Difference between revisions
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<StructureSection load='1A36' size='340' side='right' caption='Caption for this structure' scene=''> | <StructureSection load='1A36' size='340' side='right' caption='Caption for this structure' scene=''> | ||
Eukaryotic DNA topoisomerase I (topo I) is a protein that reduces the strain from the supercoils that are caused during transcription and translation<ref name="Staker">DOI 10.1073/pnas.242259599</ref>. There are two types of topoisomerases. Type 1 topoisomerases are monomeric and break one strand of DNA<ref name="Redinbo">PMID:9488644</ref>. Type 2 topoisomerases are dimeric, meaning that they made up of two units and break both strands of the DNA helix<ref name="Redinbo" />. They are able to pass another part of the duplex through the cut, and close the cut using ATP<ref name="Staker" />. | Eukaryotic DNA topoisomerase I (topo I) is a protein that reduces the strain from the supercoils that are caused during transcription and translation<ref name="Staker">DOI 10.1073/pnas.242259599</ref>. There are two types of topoisomerases. Type 1 topoisomerases are monomeric and break one strand of DNA<ref name="Redinbo">PMID:9488644</ref>. Type 2 topoisomerases are dimeric, meaning that they made up of two units and break both strands of the DNA helix<ref name="Redinbo" />. They are able to pass another part of the duplex through the cut, and close the cut using ATP<ref name="Staker" />. | ||
[[Image:04_27_21_A136_Top_1_and_Top_2_Example.jpg]]. <ref name="Dyakonov">D'yakonov, V. A., Dzhemileva, L. U., & Dzhemilev, U. M. (2017). Advances in the Chemistry of Natural and Semisynthetic Topoisomerase I/II Inhibitors. Studies in Natural Products Chemistry, 21–86. https://doi.org/10.1016/b978-0-444-63929-5.00002-4 </ref>. | |||
== Structure == | == Structure == | ||
Human topo 1 is composed of 765 amino acids <ref name="Redinbo" />. The enzyme consist of 4 regions which are the NH2-terminal, core, linker, and COOH-terminal domains<ref name="Redinbo" />. The NH2-terminal is approximately 210 residues long, it is highly charged, disordered, and contains few hydrophobic amino acids<ref name="Redinbo" />. The COOH-terminal domain is made up of residues 713 to 765 and contains the important amino aside Tyrosine 223<ref name="Redinbo"/>. The location of the active site is at this amino acid<ref name="Redinbo" />. | Human topo 1 is composed of 765 amino acids <ref name="Redinbo" />. The enzyme consist of 4 regions which are the NH2-terminal, core, linker, and COOH-terminal domains<ref name="Redinbo" />. The NH2-terminal is approximately 210 residues long, it is highly charged, disordered, and contains few hydrophobic amino acids<ref name="Redinbo" />. The COOH-terminal domain is made up of residues 713 to 765 and contains the important amino aside Tyrosine 223<ref name="Redinbo"/>. The location of the active site is at this amino acid<ref name="Redinbo" />. | ||