This is a default text for your page '. Click above on edit this page' to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia [1] or to the article describing Jmol [2] to the rescue.
Function
Structure
The alpha-synuclein (1-121) (default scene) is about 14 kDa fibril constituted by two protofilaments of 121 residues (2). The presence of many ꞵ-sheet induce a Greek-key motif of 99Å diameter(1). Indeed, There are 8 Beta-strands interrupted by glycines (Scene), between the residues 42 to about 102 (2).
Two structures coincide thanks to the presence of hydrophobic and hydrophilic regions (hydro scene). A hydrophobic intra-molecular core between the two protofilaments is formed by alanines, valines and one isoleucine. A hydrophilic channel contains majority of threonines. To stabilize the protein in an aqueous solution, there are solvent exposed charged residues : Lysine and glutamic acid.
Disease
One of the main characteristics of Neurodegenerative disorders is the loss of the protective capacity surrounding the neurons or the gain of the toxic proteins. The mechanism by which the neuronal damage occurs is due to specific mutations, or other alterations of the synaptic proteins. Recently, two main hypotheses have been developed surrounding Parkinson's disease research. Firstly, the missense mutation of the α-synuclein gene is a rare genetic disorder that cause Parkinson's disease. Secondly, the α-synuclein protein is the main component of Lewy bodies and Lewy neurites which are defining pathological characteristics of all Parkinson's disease cases.
Relevance
Structural highlights
This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
