User:Alice Harmon/Sandbox 1: Difference between revisions
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The kinase structure used in the above tour is that of the active conformation of PKA. Following is a comparison of this active conformation, with its particular arrangement of structural elements, to the inactive conformation. While active conformations of protein kinases are very similar, there is great variation in the inactive conformations of protein kinases, but all involve misalignment of one or more of the structures, subdomain III (C-helix in PKA) and the catalytic, magnesium binding, and activation loops<ref name = "TaylorTIBS"/>. | The kinase structure used in the above tour is that of the active conformation of PKA. Following is a comparison of this active conformation, with its particular arrangement of structural elements, to the inactive conformation. While active conformations of protein kinases are very similar, there is great variation in the inactive conformations of protein kinases, but all involve misalignment of one or more of the structures, subdomain III (C-helix in PKA) and the catalytic, magnesium binding, and activation loops<ref name = "TaylorTIBS"/>. | ||
<Structure load='1J3H' size='350' frame='true' align='right' caption='1j3h - apoPKA' scene='55/555705/Apopka/ | <Structure load='1J3H' size='350' frame='true' align='right' caption='1j3h - apoPKA' scene='55/555705/Apopka/2' /> | ||