English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
 
 
DownloadE-Mail
  Thermodynamic and kinetic characterization of the interaction between the Ras binding domain of AF6 and members of the Ras subfamily

Linnemann, T., Geyer, M., Jaitner, B. K., Block, C., Kalbitzer, H. R., Wittinghofer, A., et al. (1999). Thermodynamic and kinetic characterization of the interaction between the Ras binding domain of AF6 and members of the Ras subfamily. The Journal of Biological Chemistry, 274(19), 13556-13562. doi:10.1074/jbc.274.19.13556.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0024-58C8-8 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-A4CC-7
Genre: Journal Article

Files

show Files
hide Files
:
JBiolChem_274_1999_13556.pdf (Any fulltext), 177KB
 
File Permalink:
-
Name:
JBiolChem_274_1999_13556.pdf
Description:
-
Visibility:
Restricted (Max Planck Institute for Medical Research, MHMF; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show
hide
Description:
-
Description:
-

Creators

show
hide
 Creators:
Linnemann, Thomas, Author
Geyer, Matthias1, Author              
Jaitner, Birgit K., Author
Block, Christoph1, Author              
Kalbitzer, Hans Robert1, Author              
Wittinghofer, Alfred1, Author              
Herrmann, Christian, Author
Affiliations:
1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              

Content

show
hide
Free keywords: -
 Abstract: Cellular signaling downstream of Ras is highly diversified and may involve many different effector molecules. A potential candidate is AF6 which was originally identified as a fusion to ALL−1 in acute myeloid leukemia. In the present work the interaction between Ras and AF6 is characterized and compared with other effectors. The binding characteristics are quite similar to Raf and RalGEF, i.e. nucleotide dissociation as well as GTPase−activating protein activity are inhibited, whereas the intrinsic GTPase activity of Ras is unperturbed by AF6 binding. Particularly, the dynamics of interaction are similar to Raf and RalGEF with a lifetime of the Ras?AF6 complex in the millisecond range. As probed by 31P NMR spectroscopy one of two major conformational states of Ras is stabilized by the interaction with AF6. Looking at the affinities of AF6 to a number of Ras mutants in the effector region, a specificity profile emerges distinct from that of other effector molecules. This finding may be useful in defining the biological function of AF6 by selectively switching off other pathways downstream of Ras using the appropriate effector mutant. Notably, among the Ras−related proteins AF6 binds most tightly to Rap1A which could imply a role of Rap1A in AF6 regulation

Details

show
hide
Language(s): eng - English
 Dates: 1998-10-271999-01-131999-05-07
 Publication Status: Published in print
 Pages: 7
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 666554
DOI: 10.1074/jbc.274.19.13556
URI: http://www.ncbi.nlm.nih.gov/pubmed/10224125
Other: 4447
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: The Journal of Biological Chemistry
  Other : JBC
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Baltimore, etc. : American Society for Biochemistry and Molecular Biology [etc.]
Pages: - Volume / Issue: 274 (19) Sequence Number: - Start / End Page: 13556 - 13562 Identifier: ISSN: 0021-9258
CoNE: https://pure.mpg.de/cone/journals/resource/954925410826_1