User:Scott H. Vanson/Sandbox 1

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: ==DNA Polymerase θ== <StructureSection load='4x0p' size='340' side='right' caption='Caption for this structure' scene=''> This is a default text for your page '''Scott H. Vanson/Sandbox 1...)
Line 1: Line 1:
==DNA Polymerase θ==
==DNA Polymerase θ==
-
<StructureSection load='4x0p' size='340' side='right' caption='Caption for this structure' scene=''>
+
<StructureSection load='4x0p' size='340' side='right' caption='Polymerase θ polymerase domain bound to DNA''>
This is a default text for your page '''Scott H. Vanson/Sandbox 1'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
This is a default text for your page '''Scott H. Vanson/Sandbox 1'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
== General Description ==
== General Description ==
-
Human polymerase θ (pol θ) is large, 290kD enzyme consisting of three distinct domains (1,2). An N-terminal helicase-like domain, whose exact cellular functions are a topic of on-going debate and research, is linked to a C-terminal polymerase domain by a large and disordered central region (2).
+
Human polymerase θ (pol θ) is large, 290kD enzyme consisting of three distinct domains (1,2). An N-terminal helicase-like domain, whose exact cellular functions are a topic of on-going debate and research (3,4), is linked to a C-terminal, family A DNA polymerase domain by a large and disordered central region (2). Notably, pol θ is the only known human polymerase to contain a polymerase and helicase domain in one molecule (5). The focus of this page is the polymerase domain.
 +
 
 +
Pol θ is thought to promote overall genomic stability by performing several distinct cellular functions. The primary role of the enzyme is to repair of double-stranded DNA breaks as the key enzyme in an error-prone non-homologous end-joining pathway called alternative end-joining (6) or theta-mediated end-joining.
== Structural Highlights ==
== Structural Highlights ==
Line 17: Line 19:
</StructureSection>
</StructureSection>
== References ==
== References ==
 +
1. Yousefzadeh MJ, Wood RD. DNA polymerase POLQ and cellular defense against DNA damage. DNA Repair (Amst). 2013; 12:1–9. [PubMed: 23219161]
 +
2. Seki M, Marini F, Wood RD. POLQ (Pol theta), a DNA polymerase and DNA-dependent ATPase in human cells. Nucleic Acids Res. 2003; 31:6117–6126. [PubMed: 14576298]
 +
3. Sfeir RPA
 +
4. Pomerantz Helicase
 +
5. Zahn
 +
6. Yousefzadeh MJ, et al. Mechanism of Suppression of Chromosomal Instability by DNA Polymerase POLQ. PLoS Genet. 2014; 10:e1004654. [PubMed: 25275444]
<references/>
<references/>

Revision as of 16:17, 28 April 2018

DNA Polymerase θ

PDB ID 4x0p

Drag the structure with the mouse to rotate

References

1. Yousefzadeh MJ, Wood RD. DNA polymerase POLQ and cellular defense against DNA damage. DNA Repair (Amst). 2013; 12:1–9. [PubMed: 23219161] 2. Seki M, Marini F, Wood RD. POLQ (Pol theta), a DNA polymerase and DNA-dependent ATPase in human cells. Nucleic Acids Res. 2003; 31:6117–6126. [PubMed: 14576298] 3. Sfeir RPA 4. Pomerantz Helicase 5. Zahn 6. Yousefzadeh MJ, et al. Mechanism of Suppression of Chromosomal Instability by DNA Polymerase POLQ. PLoS Genet. 2014; 10:e1004654. [PubMed: 25275444]

  1. Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
  2. Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644

Proteopedia Page Contributors and Editors (what is this?)

Scott H. Vanson

Personal tools