Sandbox GGC5: Difference between revisions
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•This alternate structure highlights the <scene name='78/781193/Tyr_selection_tc/1'>Tyrosine</scene> involved in activity regulation. Full activation of the protein kinase domain requires both phosphorylation of Tyrosine to prevent it from blocking the catalytic aspartate residue, and binding of the C-terminal regulatory tail of the molecule which results in ATP binding to the kinase. | •This alternate structure highlights the <scene name='78/781193/Tyr_selection_tc/1'>Tyrosine</scene> involved in activity regulation. Full activation of the protein kinase domain requires both phosphorylation of Tyrosine to prevent it from blocking the catalytic aspartate residue, and binding of the C-terminal regulatory tail of the molecule which results in ATP binding to the kinase. | ||
•This structure view highlights the <scene name='78/781193/Titin_mutation_tc_val/2'>VAL residue 54</scene>.The VAL residue located at #54 is one of the mutations present in the cardiomyopathy,familial hypertrophic 9, disease. This VAL residue is replaced by a MET residue when the disease is present in an infected individual. <ref>PMID:10462489</ref> | |||
•This is the <scene name='78/781193/Complete_structure_tc/1'>complete titin</scene> structure. This secondary view shows multiple titin proteins connected together. This representation is known as the titin band. | •This is the <scene name='78/781193/Complete_structure_tc/1'>complete titin</scene> structure. This secondary view shows multiple titin proteins connected together. This representation is known as the titin band. | ||
