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Essential phospholipid that facilitates fat emulsification and cellular membrane breakdown

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revealed that the cyclin-dependent kinase (Cdk) inhibitor p21 Waf1/Cip1/Sdi1 lack stable secondary or tertiary structure in the free solution state, but its N-terminal region adopts an ordered stable conformation when bound to Cdk2, thereby providing a mechanical explanation to the remarkable ability of p21 Waf1/Cip1/Sdi1 to bind and inhibit a diverse family of cyclin-Cdk complexes, including cyclin A-Cdk2, cyclin E-Cdk2, and cyclin D-Cdk4 (Kriwacki et al., 1996)