User:Michael Lartey/Sandbox: Difference between revisions

Revision as of 18:44, 16 December 2008 view source Michael Lartey (talk \| contribs) 40 edits No edit summary ← Older edit		Revision as of 18:46, 16 December 2008 view source Michael Lartey (talk \| contribs) 40 edits No edit summary Newer edit →
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	'''Catalysis and Ligand Binding'''		'''Catalysis and Ligand Binding'''

	At the active center of the enzyme is a glycine-rich P-loop that connects b1 and a1 to form a giant anion hole. The hole accommodates the β-phosphoryl group of ATP, one of its natural substrates. The other natural substrate, deoxythymidine (dT), is located in the pocket formed by a3, a4 and a5. Drugs also insert into this pocket for phosphorylation. ATP binds at the giant anion hole. This active center is highly ~~reserved~~ in TKs.		At the active center of the enzyme is a glycine-rich P-loop that connects b1 and a1 to form a giant anion hole. The hole accommodates the β-phosphoryl group of ATP, one of its natural substrates. The other natural substrate, deoxythymidine (dT), is located in the pocket formed by a3, a4 and a5. Drugs also insert into this pocket for phosphorylation. ATP binds at the giant anion hole. This active center is highly conserved in TKs as shown by the consurf analysis.

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