Author Name: *THENMOZHI. M
Volume No : 1, Issue No : 1, Published year : 2014, Category : Informatics
Volume No : 1, Issue No : 1, Published year : 2014, Category : Informatics
Abstract:
Glucocorticoid induced leucine zipper protein (GILZ) is a glucocorticoid receptor responsive protein; it plays a key role in autoimmunity suppression via Rel-A domain (p-65 subunit of NF-kB) interaction. To identify the interface residues (Hot spot residues) between the interacting proteins would reveal the importance of the biological function of the complex, since they are considered being a possible ways of disrupting the proteinprotein interaction. Computational methods to study protein-protein interactions are affordable when compared to experimental alanine scanning experiments. From the results, we studied the hydrogen bond forming aminoacids between the protein-protein complexes, predicted hydrogen bond forming aminoacids between the interacting proteins, are in the range of the experimentally predicted aminoacid length. Computational methods that predict the structure and specificity of protein-protein interactions can yield deep insight into the structural biology of many biochemical pathways.
Glucocorticoid induced leucine zipper protein (GILZ) is a glucocorticoid receptor responsive protein; it plays a key role in autoimmunity suppression via Rel-A domain (p-65 subunit of NF-kB) interaction. To identify the interface residues (Hot spot residues) between the interacting proteins would reveal the importance of the biological function of the complex, since they are considered being a possible ways of disrupting the proteinprotein interaction. Computational methods to study protein-protein interactions are affordable when compared to experimental alanine scanning experiments. From the results, we studied the hydrogen bond forming aminoacids between the protein-protein complexes, predicted hydrogen bond forming aminoacids between the interacting proteins, are in the range of the experimentally predicted aminoacid length. Computational methods that predict the structure and specificity of protein-protein interactions can yield deep insight into the structural biology of many biochemical pathways.
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