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Modular PH and C2 domains in membrane attachment and other functions
Author(s) -
Katan Matilda,
Allen Victoria L
Publication year - 1999
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/s0014-5793(99)00531-1
Subject(s) - pleckstrin homology domain , modular design , function (biology) , chemistry , membrane protein , homology modeling , microbiology and biotechnology , membrane , protein structure , biochemistry , intermolecular interaction , parallels , computational biology , biophysics , biology , intermolecular force , molecule , computer science , enzyme , operating system , mechanical engineering , organic chemistry , engineering
The pleckstrin homology and C2 domains are modular protein structures involved in mediating intermolecular interactions. Although they represent distinct domains, there are several parallels regarding their function and type of interactions in which they participate. Both domains are stable structural entities that incorporate variable regions which, in different proteins, can be adapted to perform a specific function through binding to membrane phospholipids or specific protein ligands. A number of recent examples illustrate the function of some of these domains in regulated membrane attachment, with an important role in many cellular signalling pathways.