Merk, S. Banerjee, D. Matthies, X. Wu, J. Subramaniam 2. Science , Juers, B. Huber LacZ beta-galactosidase: structure and function of an enzyme of historical and molecular biological importance. Protein Science 21, Juers, T. Heightman, A. Vasella, J. McCarter, L. Mackenzie, S.
Matthews A structural view of the action of Escherichia coli lacZ beta-galactosidase. Biochemistry 40, About Molecule of the Month. Each installment includes an introduction to the structure and function of the molecule, a discussion of the relevance of the molecule to human health and welfare, and suggestions for how visitors might view these structures and access further details. Keratan sulfate belongs to a group of large sugar molecules called glycosaminoglycans GAGs or mucopolysaccharides.
The GLB1 gene also provides instructions for making the elastin-binding protein. On the cell surface, elastin-binding protein interacts with proteins called cathepsin A and neuraminidase 1 to form the elastin receptor complex. This receptor complex plays a role in the formation of elastic fibers, which are a component of the connective tissue that forms the body's supportive framework. As a result, these substances accumulate to toxic levels in many tissues and organs.
In the brain, progressive damage caused by the buildup of GM1 ganglioside leads to the destruction of nerve cells, which causes many of the signs and symptoms of GM1 gangliosidosis.
Although the role elastin-binding protein plays in the development of GM1 gangliosidosis is unclear, the alteration of this protein may contribute to the weakened heart muscle cardiomyopathy found in some people with GM1 gangliosidosis. Most of these mutations change single nucleotides in the gene.
The degradation of GM1 ganglioside is not affected by these mutations. Because keratan sulfate is predominantly found in cartilage and the cornea, the buildup of this substance causes skeletal abnormalities and cloudy corneas.
Researchers believe that a buildup of GAGs may also cause the features of MPS IV by interfering with the functions of other proteins inside lysosomes and disrupting the movement of molecules inside the cell. International Journal of Molecular Sciences , 22 8 , Process Biochemistry , , Computational and Structural Biotechnology Journal , 19 , Sobolev , Pavel V.
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