Harjes, E.; Harjes, S.; Wohlgemuth, S.; Mueller, K.H.; Krieger, E.; Herrmann, C.; Bayer, Peter:
GTP-Ras disrupts the intramolecular complex of C1 and RA domains of Nore1.
In: Structure, Band 14 (2006), S. 881 - 888
2006Artikel/Aufsatz in ZeitschriftOA Embargo
Biologie
Damit verbunden: 1 Publikation(en)
Titel in Englisch:
GTP-Ras disrupts the intramolecular complex of C1 and RA domains of Nore1.
Autor*in:
Harjes, E.;Harjes, S.
Sonstiges
korrespondierende*r Autor*in
;
Wohlgemuth, S.;Mueller, K.H.;Krieger, E.;Herrmann, C.;Bayer, PeterUDE
GND
1059319691
LSF ID
10134
ORCID
0000-0003-0435-7202ORCID iD
Sonstiges
der Hochschule zugeordnete*r Autor*in
Erscheinungsjahr:
2006
Open Access?:
OA Embargo
PubMed ID
Sprache des Textes:
Englisch
Ressourcentyp:
Text

Abstract in Englisch:

The novel Ras effector mNore1, capable of inducing apoptosis, is a multidomain protein. It comprises a C1 domain homologous to PKC and an RA domain similar to the Ras effectors AF-6 and RalGDS. Here, we determine the affinity of these two domains to the active forms of Ras and Rap1 using isothermal calorimetric titration. The interaction of Ras/Rap1-GTP with the RA domain of mNore1 is weakened significantly by direct binding of the C1 domain to the RA domain. In order to analyze this observation in atomic detail, we solved the C1 solution structure by NMR. By determining chemical shifts and relaxation rates, we can show an intramolecular complex of C1-RA. GTP-Ras titration and binding to RA disrupts this complex and displaces the C1 domain. Once the C1 domain tumbles freely in solution, a lipid binding interface becomes accessible. Furthermore, we provide evidence of phosphatidylinositol 3-phosphate binding of the free C1 domain.