Journal
FEBS LETTERS
Volume 586, Issue 17, Pages 2662-2673Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2012.06.006
Keywords
Signal transduction; Protein structure; Protein complex; Signaling domain; X-ray crystallography; G-Protein; Protein fold; Signal regulator
Funding
- Peter and Traudl Engelhorn Foundation (Penzberg, Germany)
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The initial reports on pleckstrin homology (PH) domains almost 20 years ago described them as sequence feature of proteins involved in signal transduction processes. Investigated at first along the phospholipid binding properties of a small subset of PH representatives, the PH fold turned out to appear as mediator of phosphotyrosine and polyproline peptide binding to other signaling proteins. While phospholipid binding now seems rather the exception among PH-like domains, protein-protein interactions established as more and more important feature of these modules. In this review we focus on the PH superfold as a versatile protein-protein interaction platform and its three-dimensional integration in an increasing number of available multidomain structures. (C) 2012 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.
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