5N4W
Crystal structure of the Cul2-Rbx1-EloBC-VHL ubiquitin ligase complex
Summary for 5N4W
| Entry DOI | 10.2210/pdb5n4w/pdb |
| Descriptor | Cullin-2, Von Hippel-Lindau disease tumor suppressor, E3 ubiquitin-protein ligase RBX1, ... (6 entities in total) |
| Functional Keywords | cullin ring, e3 ubiquitin ligase, vhl, ligase, cullin-2 |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 5 |
| Total formula weight | 140376.78 |
| Authors | Cardote, T.A.F.,Gadd, M.S.,Ciulli, A. (deposition date: 2017-02-11, release date: 2017-06-07, Last modification date: 2024-05-01) |
| Primary citation | Cardote, T.A.F.,Gadd, M.S.,Ciulli, A. Crystal Structure of the Cul2-Rbx1-EloBC-VHL Ubiquitin Ligase Complex. Structure, 25:901-911.e3, 2017 Cited by PubMed Abstract: Cullin RING E3 ubiquitin ligases (CRLs) function in the ubiquitin proteasome system to catalyze the transfer of ubiquitin from E2 conjugating enzymes to specific substrate proteins. CRLs are large dynamic complexes and attractive drug targets for the development of small-molecule inhibitors and chemical inducers of protein degradation. The atomic details of whole CRL assembly and interactions that dictate subunit specificity remain elusive. Here we present the crystal structure of a pentameric CRL2 complex, composed of Cul2, Rbx1, Elongin B, Elongin C, and pVHL. The structure traps a closed state of full-length Cul2 and a new pose of Rbx1 in a trajectory from closed to open conformation. We characterize hotspots and binding thermodynamics at the interface between Cul2 and pVHL-EloBC and identify mutations that contribute toward a selectivity switch for Cul2 versus Cul5 recognition. Our findings provide structural and biophysical insights into the whole Cul2 complex that could aid future drug targeting. PubMed: 28591624DOI: 10.1016/j.str.2017.04.009 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.9 Å) |
Structure validation
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