PMID:8236453
| Citation |
Musacchio, A, Gibson, T, Rice, P, Thompson, J and Saraste, M (1993) The PH domain: a common piece in the structural patchwork of signalling proteins. Trends Biochem. Sci. 18:343-8 |
|---|---|
| Abstract |
The 'pleckstrin homology' domain is an approximately 100-residue protein module that has recently been added to the domain catalogue of signalling proteins. For this review we have made an extensive database search using a profile search method, and found a number of additional proteins that may contain PH domains. The PH domain is present in many kinases, isoforms of phospholipase C, GTPases, GTPase-activating proteins and nucleotide-exchange factors, including such proteins as Vav, Dbl and Bcr, and there are two PH domains in a guanine-nucleotide releasing factor of Ras. Many PH-domain-containing proteins interact with GTP-binding proteins. We have also identified a PH domain in beta-adrenergic receptor kinase exactly in the region that has already been shown to be involved in binding to the beta and gamma subunits of a heterotrimeric G protein. This suggests that PH domains may be involved in interactions with GTP-binding proteins. |
| Links | |
| Keywords |
Amino Acid Sequence; Animals; Blood Proteins/chemistry; Blood Proteins/metabolism; GTP-Binding Proteins/metabolism; Humans; Molecular Sequence Data; Phosphoproteins; Sequence Homology, Amino Acid; Signal Transduction |
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