English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  The PH domain: a common piece in the structural pathcwork of signalling proteins

Musacchio, A., Gibson, T., Rice, P., Thompson, J., & Saraste, M. (1993). The PH domain: a common piece in the structural pathcwork of signalling proteins. TRENDS IN BIOCHEMICAL SCIENCES, 18(9), 343-348. doi:10.1016/0968-0004(93)90071-T.

Item is

Files

show Files

Locators

show

Creators

show
hide
 Creators:
Musacchio, Andrea1, Author           
Gibson, Toby2, Author
Rice, Peter2, Author
Thompson, Julie2, Author
Saraste, Matti2, Author
Affiliations:
1Abt. I:Mechanistische Zellbiologie, Max Planck Institute of Molecular Physiology, Max Planck Society, ou_1753287              
2European Molecular Biology Laboratory, Meyerhofstrasse 1, D-69012 Heidelberg, Germany, ou_persistent22              

Content

show
hide
Free keywords: -
 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.

Details

show
hide
Language(s):
 Dates: 1993
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: TRENDS IN BIOCHEMICAL SCIENCES
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 18 (9) Sequence Number: - Start / End Page: 343 - 348 Identifier: ISSN: 0968-0004