9SNF
CTLH-CRA domain of murine RanBP10
Summary for 9SNF
| Entry DOI | 10.2210/pdb9snf/pdb |
| Descriptor | Ran-binding protein 10 (2 entities in total) |
| Functional Keywords | ctlh complex, gid complex, e3 ligase, ligase |
| Biological source | Mus musculus (house mouse) More |
| Total number of polymer chains | 2 |
| Total formula weight | 33059.34 |
| Authors | van gen Hassend, P.M.,Schindelin, H. (deposition date: 2025-09-10, release date: 2026-02-18, Last modification date: 2026-09-02) |
| Primary citation | van gen Hassend, P.M.,Schindelin, H. A structural code for assembly specificity in GID/CTLH-type E3 ligases. Elife, 15:-, 2026 Cited by PubMed Abstract: GID/CTLH-type E3 ligases assemble into conserved ring-shaped architectures built from repeating LisH-CTLH-CRA modules, yet the molecular rules that enforce their highly specific subunit arrangement have remained unknown. Here, we decode the structural 'assembly specificity code' that governs CRA-CRA pairing. Using crystal structures of multiple CTLH-CRA domains, including the RanBP9-muskelin heterodimer, integrated with quantitative binding analyses, we show that several interfaces operate with exceptionally high affinity, reaching the picomolar range, and that conserved sequence and geometric features enable each subunit to only select cognate partners. Strikingly, targeted perturbations of these features are sufficient to reprogram pairing preferences, enabling engineered subunits such as RanBP10 or Twa1 to adopt non-native interaction partners. These findings reveal the molecular logic that preserves the architecture of GID/CTLH-type E3 ligases and demonstrate that their assembly code is both decipherable and engineerable, providing a conceptual foundation for reconfiguring these ring-shaped E3 ligases. PubMed: 41948802DOI: 10.7554/eLife.110152 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.07 Å) |
Structure validation
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