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The three-dimensional structure of human tissue inhibitor of metalloproteinases-2 (TIMP-2) was determined by X-ray crystallography to 2.1 A resolution. The structure of the inhibitor consists of two domains. The N-terminal domain (residues 1-110) is folded into a β-barrel, similar to the oligonucleotide/oligosaccharide binding fold otherwise found in certain DNA-binding proteins. The C-terminal domain...
Background: The four members of the INK4 gene family (p16 INK4a , p15 INK4b , p18 INK4c and p19 INK4d ) inhibit the closely related cyclin-dependent kinases CDK4 and CDK6 as part of the regulation of the G 1 ->S transition in the cell-division cycle. Loss of INK4 gene product...
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