Mechanistic insights into phosphoprotein-binding FHA domains.
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ABSTRACT: [Structure: see text]. FHA domains are protein modules that switch signals in diverse biological pathways by monitoring the phosphorylation of threonine residues of target proteins. As part of the effort to gain insight into cellular avoidance of cancer, FHA domains involved in the cellular response to DNA damage have been especially well-characterized. The complete protein where the FHA domain resides and the interaction partners determine the nature of the signaling. Thus, a key biochemical question is how do FHA domains pick out their partners from among thousands of alternatives in the cell? This Account discusses the structure, affinity, and specificity of FHA domains and the formation of their functional structure. Although FHA domains share sequence identity at only five loop residu
SUBMITTER: Liang X
PROVIDER: S-EPMC2962622 | biostudies-literature | 2008 Aug
REPOSITORIES: biostudies-literature
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