2FNF
C1 domain of Nore1
Summary for 2FNF
| Entry DOI | 10.2210/pdb2fnf/pdb |
| Related | 1RFH |
| Descriptor | putative Ras Effector Nore1, ZINC ION (2 entities in total) |
| Functional Keywords | zinc; signal transduction; apoptosis; cysteine rich domain, apoptosis |
| Biological source | Mus musculus (house mouse) |
| Total number of polymer chains | 1 |
| Total formula weight | 8400.34 |
| Authors | Harjes, E.,Harjes, S.,Wohlgemuth, S.,Krieger, E.,Herrmann, C.,Muller, K.H.,Bayer, P. (deposition date: 2006-01-11, release date: 2006-02-07, Last modification date: 2024-05-29) |
| Primary citation | Harjes, E.,Harjes, S.,Wohlgemuth, S.,Muller, K.H.,Krieger, E.,Herrmann, C.,Bayer, P. GTP-Ras disrupts the intramolecular complex of C1 and RA domains of Nore1. Structure, 14:881-888, 2006 Cited by PubMed Abstract: 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. PubMed: 16698549DOI: 10.1016/j.str.2006.03.008 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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