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Title
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GTP plus water mimic ATP in the active site of protein kinase CK2.
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Authors
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K.Niefind,
M.Pütter,
B.Guerra,
O.G.Issinger,
D.Schomburg.
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Ref.
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Nat Struct Biol, 1999,
6,
1100-1103.
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PubMed id
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Abstract
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The structures of the catalytic subunit of protein kinase CK2 from Zea mays
complexed with Mg2+ and with analogs of ATP or GTP were determined to 2.2 A
resolution. Unlike most other protein kinases, CK2 from various sources shows
'dual-cosubstrate specificity', that is, the ability to efficiently use either
ATP or GTP as a cosubstrate. The structures of these complexes demonstrate that
water molecules are critical to switch the active site of CK2 from an ATP- to a
GTP-compatible state. An understanding of the structural basis of
dual-cosubstrate specificity may help in the design of drugs that target CK2 or
other kinases with this property.
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