We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

User:Erin May/Sandbox 1

From Proteopedia

< User:Erin May
Revision as of 01:50, 26 November 2012 by Erin May (Talk | contribs)
Jump to: navigation, search

Contents

Prions as a disease causing agent

Human Prion Protein in dimer form 1i4m
Human Prion Protein in dimer form 1i4m

Image:Http://www.proteopedia.org/wiki/index.php/Image:10131 lores.jpg

Image:Http://www.proteopedia.org/wiki/index.php/Image:10131 lores.jpg
Caption: Holes in this sponge like brain tissue result from pockets of prion aggregation [1]

Prions are infectious or genetic misfolded proteins which act as templates upon which properly folded prion protein monomers can aggregate. Prions contain no nucleic acid such as other infectoius molecules or organisms. Human Prion Protein or Major Prion protein, exists as a normal constituent of human cells, found mostly in the brain[2] and is called PrPC.[3] PrPC is composed of mostly helix whereas the infectious form, PrP^Sc, is composed of high percentage beta sheets.[3]

The diseases prions confer are neurodegenerative disorders which result from the large scale aggregation of these proteins. For more information about the infections related to prions see Transmissible spongiform encephalopathy at Wikipedia.


Unfolding Mechanism

Currently, the mechanism by which a template prion unfolds a the helices of a properly folded prion protein is unknown. Specific residues have been shown to either confer resistance or lend themselves to this unfolding.

PrPC natural monomer

Image:1qlx.png
Human Prion Protein in dimer form 1qlx[4]

Structure of Yeast Poly(A) Polymerase with ATP and oligo(A) (PDB entry 2q66)

Drag the structure with the mouse to rotate

Dimer and Full aggregate forms

Reference List

  1. ↑ Image of Creutzfeldt-Jakob positive brain tissue was obtained from The CDC's Public Health Image Library.
  2. ↑ Centers for Disease Control and Prevention
  3. ↑ 3.0 3.1 Prusiner SB. Prions. Proc Natl Acad Sci U S A. 1998 Nov 10;95(23):13363-83. PMID:9811807
  4. ↑ Fiegel P. [Current diagnostic methods: the value of urine analysis]. Fortschr Med. 1978 Jun 8;96(22):1177-80 PMID:26630

Proteopedia Page Contributors and Editors (what is this?)

Erin May, Jaime Prilusky

Retrieved from "http://52.214.119.220/wiki/index.php/User:Erin_May/Sandbox_1"
Personal tools