Premium
Pleckstrin homology (PH) like domains – versatile modules in protein–protein interaction platforms
Author(s) -
Scheffzek Klaus,
Welti Stefan
Publication year - 2012
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2012.06.006
Subject(s) - pleckstrin homology domain , protein–protein interaction , polyproline helix , biochemistry , chemistry , homology (biology) , plasma protein binding , mediator , peptide sequence , sequence homology , protein structure , computational biology , signal transduction , microbiology and biotechnology , biology , peptide , amino acid , gene
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.