2LQW
Solution structure of phosphorylated CRKL
Summary for 2LQW
| Entry DOI | 10.2210/pdb2lqw/pdb |
| NMR Information | BMRB: 18333 |
| Descriptor | Crk-like protein (1 entity in total) |
| Functional Keywords | sh2, sh3, v-crk sarcoma virus ct10, oncogene homolog, (avian)-like, pcrkl, signaling protein |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 33896.89 |
| Authors | Jankowski, W.,Saleh, T.,Kalodimos, C. (deposition date: 2012-03-16, release date: 2012-05-16, Last modification date: 2023-06-14) |
| Primary citation | Jankowski, W.,Saleh, T.,Pai, M.T.,Sriram, G.,Birge, R.B.,Kalodimos, C.G. Domain organization differences explain Bcr-Abl's preference for CrkL over CrkII. Nat.Chem.Biol., 8:590-596, 2012 Cited by PubMed Abstract: CrkL is a key signaling protein that mediates the leukemogenic activity of Bcr-Abl. CrkL is thought to adopt a structure that is similar to that of its CrkII homolog. The two proteins share high sequence identity and indistinguishable ligand binding preferences, yet they have distinct physiological roles. Here we show that the structures of CrkL and phosphorylated CrkL are markedly different than the corresponding structures of CrkII. As a result, the binding activities of the Src homology 2 and Src homology 3 domains in the two proteins are regulated in a distinct manner and to a different extent. The different structural architecture of CrkL and CrkII may account for their distinct functional roles. The data show that CrkL forms a constitutive complex with Abl, thus explaining the strong preference of Bcr-Abl for CrkL. The results also highlight how the structural organization of the modular domains in adaptor proteins can control signaling outcome. PubMed: 22581121DOI: 10.1038/nchembio.954 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
