Sandbox Reserved 312

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 4: Line 4:
{{STRUCTURE_2fbv| PDB=2fbv | SCENE= }}
{{STRUCTURE_2fbv| PDB=2fbv | SCENE= }}
-
Werner (WRN) protein is one of the five human RecQDNA helicases. This enzyme has a helicases function (unwinding the DNA helix) and a nuclease function (degrading), which allows for deletion of mutation and proofreading. The WRN has a functional exonuclease domain located on the N-terminus. WRN protein protects human from cancer; as well as, premature aging.
+
Werner (WRN) protein is a member of the human RecQDNA helicases. This enzyme has a helicases function (unwinding double-stranded DNA helix in the 3'-5' direction) and a exonuclease activity (degrading), which allows for deletion of mutation and proofreading. The WRN has a functional exonuclease domain located on the N-terminus. WRN protein protects human from cancer; as well as, premature aging.
Line 13: Line 13:
=Structure=
=Structure=
 +
The WRN protein is built from several individual WRN copies.
The WRN protein is built from several individual WRN copies.
 +
The exonuclease region of the protein is located at the N-terminal end with 171 amino acids. They form a hexamer around the end of the strand when exposed to double strand DNA, which is essential to DNA repair of the WRN.
WRN is a enzyme with both magnesium and ATP-dependent DNA-helicase activity with a 3'->5' exonuclease
WRN is a enzyme with both magnesium and ATP-dependent DNA-helicase activity with a 3'->5' exonuclease
activity towards double-stranded DNA. <ref name= "Perry"> PMID: 16622405 </ref>
activity towards double-stranded DNA. <ref name= "Perry"> PMID: 16622405 </ref>

Revision as of 02:53, 3 April 2011

This Sandbox is Reserved from January 10, 2010, through April 10, 2011 for use in BCMB 307-Proteins course taught by Andrea Gorrell at the University of Northern British Columbia, Prince George, BC, Canada.
To get started:
  • Click the edit this page tab at the top. Save the page after each step, then edit it again.
  • Click the 3D button (when editing, above the wikitext box) to insert Jmol.
  • show the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page.
  • Add a description of your scene. Use the buttons above the wikitext box for bold, italics, links, headlines, etc.

More help: Help:Editing


PDB ID 2fbv

Drag the structure with the mouse to rotate
2fbv, resolution 2.40Å ()
Ligands:
Gene: WRN, RECQ3, RECQL2 (Homo sapiens)
Related: 2fbt, 2fbx, 2fby, 2fc0
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml


Werner (WRN) protein is a member of the human RecQDNA helicases. This enzyme has a helicases function (unwinding double-stranded DNA helix in the 3'-5' direction) and a exonuclease activity (degrading), which allows for deletion of mutation and proofreading. The WRN has a functional exonuclease domain located on the N-terminus. WRN protein protects human from cancer; as well as, premature aging.


Contents

Function

This protein plays a major role in DNA metabolic pathway, which perform DNA replication, recombination, and repair.. WRN has activity of ATPase, helicases and exonuclease. [1] WRN exonuclease functions on different structures of a DNA substrate.[2] However, WRN exonuclease can be blocked by oxidatively induced base lesion (damaged by disease tissue). The homodimer protein Ku binds to the broken double-stranded DNA, stimulating the WRN exonuclease to bypass the lesion. However, in non-digested strands the process is blocked by the lesion.

Structure

The WRN protein is built from several individual WRN copies. The exonuclease region of the protein is located at the N-terminal end with 171 amino acids. They form a hexamer around the end of the strand when exposed to double strand DNA, which is essential to DNA repair of the WRN. WRN is a enzyme with both magnesium and ATP-dependent DNA-helicase activity with a 3'->5' exonuclease activity towards double-stranded DNA. [2]


Active Site

A six membered WRN ring is formed to fit around the DNA helix. The exonuclease active site and point inward towards the DNA.

Substrate-Binding Site

Clinical significance

The build up of oxidatively induced base in DNA the gene coding for WRN is mutated a autosomal recessive disorder causing rapid aging(osteoporosis, atherosclerosis and cancer). This is known as Werner syndrome which appears at puberty.

Reference

  1. ↑ Perry JJ, Yannone SM, Holden LG, Hitomi C, Asaithamby A, Han S, Cooper PK, Chen DJ, Tainer JA. WRN exonuclease structure and molecular mechanism imply an editing role in DNA end processing. Nat Struct Mol Biol. 2006 May;13(5):414-22. Epub 2006 Apr 23. PMID:16622405 doi:http://dx.doi.org/10.1038/nsmb1088
  2. ↑ 2.0 2.1 Perry JJ, Yannone SM, Holden LG, Hitomi C, Asaithamby A, Han S, Cooper PK, Chen DJ, Tainer JA. WRN exonuclease structure and molecular mechanism imply an editing role in DNA end processing. Nat Struct Mol Biol. 2006 May;13(5):414-22. Epub 2006 Apr 23. PMID:16622405 doi:http://dx.doi.org/10.1038/nsmb1088

<references/"Bukowy"/WRN Exonuclease activity is blocked by specific oxidatively induced base lesions positioned in either DNA strand>

Retrieved from "http://52.214.119.220/wiki/index.php/Sandbox_Reserved_312"
Personal tools