Biological Regulation via Ankyrin Repeat Folding

被引:7
作者
Barrick, Doug [1 ]
机构
[1] Johns Hopkins Univ, TC Jenkins Dept Biophys, Baltimore, MD 21218 USA
关键词
CDK INHIBITOR P19(INK4D); KAPPA-B-ALPHA; CRYSTAL-STRUCTURE; CELL-CYCLE; PROTEIN; NOTCH; STABILITY; COMPLEX; DOMAIN; COOPERATIVITY;
D O I
10.1021/cb900003f
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
By mimicking the phosphorylation of p19(INK4d), a tumor suppressor containing five ankyrin repeats, the native state could be destabilized to such an extent that only a partially folded state is populated at physiological temperature. This partly folded state, which mimics an on-pathway folding intermediate lacking structure in ankyrin repeats 1 and 2, is more rapidly ubiquitinated than the parent construct. Thus, phosphorylation of p(19INK4d) is likely to regulate cell-cycle progression through both biochemical (proteasomal) and biophysical (folding and binding to cyclin-dependent kinases) mechanisms.
引用
收藏
页码:19 / 22
页数:4
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