Sandbox Reserved 815: Difference between revisions
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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. | 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:// | 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. | ||
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==Tertiary structure== | ==Tertiary structure== | ||
Between the Cysteine 179 and the Cysteine 214 we can find a <scene name='56/568013/B/1'>disulphide bound</scene> which links helix 2 and the helix 3. | Between the Cysteine 179 and the Cysteine 214 we can find a <scene name='56/568013/B/1'>disulphide bound</scene> which links helix 2 and the helix 3. | ||
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[[Image:Vjvk.jpg|center|400px||thumb|'''Structure of 3HAF domain''']] | [[Image:Vjvk.jpg|center|400px||thumb|'''Structure of 3HAF domain''']] | ||
{{STRUCTURE_3haf| PDB=3haf | SCENE= }} | |||
==Quaternary structure== | ==Quaternary structure== | ||
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<scene name='User:Erin_May/Sandbox_1/Hydrogen_bonding/1'> Arg 220 and Ser 132</scene> form a Hydrogen bond located at the end of helix 3 which permit the inter-chain interactions to be specific. | <scene name='User:Erin_May/Sandbox_1/Hydrogen_bonding/1'> Arg 220 and Ser 132</scene> form a Hydrogen bond located at the end of helix 3 which permit the inter-chain interactions to be specific. | ||