Sandbox GGC10
Lysozyme C (1RE2), a human lysosome labelled with two 2’,3’-epoxypropyl beta-glycoside of n-acetyllactosamine
This is a default text for your page Sandbox GGC10. 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. FunctionThis protein has primarily a bacteriolytic function. The lysozymes in tissues and body fluids can be commonly associated with the monocyte-macrophage system and they can also enhance the activity of the immunoagents. Lysozyme C has the capability to perform both hydrolysis and transglycosylation. It also shows a little bit of esterase activity. Lysozyme C can act rapidly on both peptide-substituted and unsubstituted peptidoglycan, but it acts slowly on chitin oligosaccharides. This protein has some catalytic activity too. There is hydrolysis of 1->4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine leaves a residue in a peptidoglycan and between N-acetyl-D-glucosamine has a residue in chitodextrins. DiseaseThis protein is involved in the disease called Amyloidosis 8 (AMYL8). This disease is caused by a mutation that affects the gene on the lysozyme C. The description of this disease states that it is a form of a hereditary generalized amyloidosis. It is clinically featured including extensive visceral amyloid deposits, renal amyloidosis resulting in nephrotic syndrome, arterial hypertension, hepatosplenomegaly, cholestasis, and petechial skin rash. This disease is not involved with the nervous system. RelevanceStructural highlightsThis is a sample scene created with SAT to color by Group, and another to make a transparent representation of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
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