Sandbox Reserved 815: Difference between revisions

Prions, misfolded proteins, are responsible of the transmissible spongiform encephalopathy in mammals. The primitive protein is involved in the cell differentiation and adhesion. In humans, prions cause. In humans, prions cause [http://en.wikipedia.org/wiki/Creutzfeldt%E2%80%93Jakob_disease Creutzfeldt-Jakob Disease](CJD), [http://en.wikipedia.org/wiki/Fatal_familial_insomnia Fatal Familial Insomnia](FFI) and [http://en.wikipedia.org/wiki/Kuru_%28disease%29 kuru].

Human prion is a membrane protein of 16284.86 Da. The infectious agent penetrates the neuron and due to reasons and mechanisms still misunderstood, it multiplies, by opening/folding normal proteins in pathogenic prions. This new form cannot be degraded by proteolysis and the aggregation of misfiled proteins induces the death of cells and the accumulation of amyloid plaque in the brain.

3HAF is a vaiant domain of the major [http://www.proteopedia.org/wiki/index.php/Human_Prion_Protein_Dimer prion]protein going from residue 90 to 231, which is constitute of 253 amino acids. Compare to the sequence of the major prion protein, a Valine substitutes a Methionine at the 129 residue, influencing the susceptibility of the formation of the prion.