期刊
CURRENT OPINION IN STRUCTURAL BIOLOGY
卷 14, 期 6, 页码 700-705出版社
CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2004.10.011
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During the past year, crystal structures of the PDK-1, ITK, Aurora-A, c-KIT and FLT-3 protein kinases in complex with several ATP-competitive inhibitors have been determined. Some structures have crystallized in catalytically active conformations, whereas others appear to be in inactive or native conformations. The differences between these two classes of structures provide further understanding of how kinase activity may be self-regulated in the cellular environment and how phosphorylation can modulate signalling at a molecular level. All of these structures provide a basis for designing selective protein kinase inhibitors of use in the treatment of cancer and autoimmune disease.
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