Journal
CURRENT OPINION IN STRUCTURAL BIOLOGY
Volume 16, Issue 6, Pages 676-685Publisher
CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2006.10.008
Keywords
-
Categories
Ask authors/readers for more resources
To achieve high biological specificity, protein kinases and phosphatases often recognize their targets through interactions that occur outside of the active site. Although the role of modular protein-protein interaction domains in kinase and phosphatase signaling has been well characterized, it is becoming clear that many kinases and phosphatases utilize docking interactions - recognition of a short peptide motif in target partners by a groove on the catalytic domain that is separate from the active site. Docking is particularly prevalent in serine/threonine kinases and phosphatases, and is a versatile organizational tool for building complex signaling networks; it confers a high degree of specificity and, in some cases, allosteric regulation.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available