Sandbox GGC15: Difference between revisions

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==DNA TOPOISOMERASE I==
==DNA TOPOISOMERASE I==
<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 et al., 2002">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 et al., 1998">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 et al., 1998" />. They are able to pass another part of the duplex through the cut, and close the cut using ATP<ref name="Staker et al., 2002" />.  
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" />.  


== Structure ==
== Structure ==
Human topo 1 is composed of 765 amino acids <ref name="Redinbo et al., 1998" />. The enzyme consist of 4 regions which are the NH2-terminal, core, linker, and COOH-terminal domains<ref name="Redinbo et al., 1998" />. The NH2-terminal  is aprroximately 210 residues long, it is highly charged, disordered, and contains few hydrophobic amino acids<ref name="Redinbo et al., 1998" />. The COOH-terminal domain is made up of residues 713 to 765 and contains the important amino aside Tyrosine 223<ref name="Redinbo et al., 1998" />. The location of the active site is at this amino acid<ref name="Redinbo et al., 1998" />. The active site is catalytic and forms a phosphoester bond with the 3' phosphate at the site of cleavage on the DNA strand<ref name="Redinbo et al., 1998" />.
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" />.  
== Disease ==
== Active Site ==
 
Topo1 reduces stress in DNA by causing breaks in the DNA helix
The active site is catalytic and forms a phosphoester bond with the 3' phosphate at the site of cleavage on the DNA strand<ref name="Redinbo" />.
== Relevance ==
== Relevance ==
Many anticancer drugs target topo 1 enzymes.
Many anticancer drugs target topo 1 enzymes.

Revision as of 00:12, 28 April 2021

DNA TOPOISOMERASE IDNA TOPOISOMERASE I

Eukaryotic DNA topoisomerase I (topo I) is a protein that reduces the strain from the supercoils that are caused during transcription and translation[1]. There are two types of topoisomerases. Type 1 topoisomerases are monomeric and break one strand of DNA[2]. Type 2 topoisomerases are dimeric, meaning that they made up of two units and break both strands of the DNA helix[2]. They are able to pass another part of the duplex through the cut, and close the cut using ATP[1].

Structure

Human topo 1 is composed of 765 amino acids [2]. The enzyme consist of 4 regions which are the NH2-terminal, core, linker, and COOH-terminal domains[2]. The NH2-terminal is approximately 210 residues long, it is highly charged, disordered, and contains few hydrophobic amino acids[2]. The COOH-terminal domain is made up of residues 713 to 765 and contains the important amino aside Tyrosine 223[2]. The location of the active site is at this amino acid[2].

Active Site

Topo1 reduces stress in DNA by causing breaks in the DNA helix

The active site is catalytic and forms a phosphoester bond with the 3' phosphate at the site of cleavage on the DNA strand[2].

Relevance

Many anticancer drugs target topo 1 enzymes.

Structural highlights

This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.


Caption for this structure

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ReferencesReferences

  1. ↑ 1.0 1.1 Staker BL, Hjerrild K, Feese MD, Behnke CA, Burgin AB Jr, Stewart L. The mechanism of topoisomerase I poisoning by a camptothecin analog. Proc Natl Acad Sci U S A. 2002 Nov 26;99(24):15387-92. Epub 2002 Nov 8. PMID:12426403 doi:10.1073/pnas.242259599
  2. ↑ 2.0 2.1 2.2 2.3 2.4 2.5 2.6 2.7 Redinbo MR, Stewart L, Kuhn P, Champoux JJ, Hol WG. Crystal structures of human topoisomerase I in covalent and noncovalent complexes with DNA. Science. 1998 Mar 6;279(5356):1504-13. PMID:9488644

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