Please note that eDoc will be permanently shut down in the first quarter of 2021!      Home News About Us Contact Contributors Disclaimer Privacy Policy Help FAQ

Home
Search
Quick Search
Advanced
Fulltext
Browse
Collections
Persons
My eDoc
Session History
Login
Name:
Password:
Documentation
Help
Support Wiki
Direct access to
document ID:


          Institute: MPI für medizinische Forschung     Collection: Abteilung Biophysik     Display Documents



ID: 565672.0, MPI für medizinische Forschung / Abteilung Biophysik
Structure of the Ras−binding domain of RalGEF and implications for Ras binding and signalling
Translation of Title:Structure of the Ras−binding domain of RalGEF and implications for Ras binding and signalling
Authors:Geyer, Matthias; Herrmann, Christine; Wohlgemuth, Sabine; Wittinghofer, Alfred; Kalbitzer, Hans Robert
Language:English
Date of Publication (YYYY-MM-DD):1997-09-01
Title of Journal:Nature Structural and Molecular Biology
Journal Abbrev.:Nat. Struct. Mol. Biol.
Volume:4
Issue / Number:9
Start Page:694
End Page:699
Review Status:Peer-review
Audience:Experts Only
Intended Educational Use:No
Abstract / Description:The solution structure of the Ras−binding domain (RBD) of Ral guanine−nucleotide exchange factor RalGEF was solved by NMR spectroscopy. The overall structure is similar to that of Raf−RBD, another effector of Ras, although the sequence identity is only 13%. 15N chemical shifts changes in the complex of RalGEF−RBD with Ras indicate an interaction similar to the intermolecular beta−sheet observed for the complex between Ras and Raf−RBD
Last Change of the Resource (YYYY-MM-DD):--
External Publication Status:published
Document Type:Article
Communicated by:Wulf Kaiser
Affiliations:MPI für medizinische Forschung/Abteilung Biophysik
MPI für medizinische Forschung/Abteilung Biomedizinische Optik
MPI für medizinische Forschung/Abteilung Biomedizinische Optik/Gruppe Moritz Helmstaedter
Identifiers:LOCALID:5427
URI:http%3A%2F%2Fwww.nature.com%2Fnsmb%2Fjournal%2Fv4%...
URI:http%3A%2F%2Fwww.nature.com%2Fnsmb%2Fjournal%2Fv4%...
DOI:10.1038%2Fnsb0997-694
Full Text:
Sorry, no privileges
The scope and number of records on eDoc is subject to the collection policies defined by each institute - see "info" button in the collection browse view.