6CCR
Selenomethionyl derivative of a GID4 fragment
Summary for 6CCR
| Entry DOI | 10.2210/pdb6ccr/pdb |
| Descriptor | Glucose-induced degradation protein 4 homolog, UNKNOWN ATOM OR ION (3 entities in total) |
| Functional Keywords | structural genomics, structural genomics consortium, sgc, protein binding |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 21786.07 |
| Authors | Dong, C.,Tempel, W.,Bountra, C.,Arrowsmith, C.H.,Edwards, A.M.,Min, J.,Structural Genomics Consortium (SGC) (deposition date: 2018-02-07, release date: 2018-04-04, Last modification date: 2024-11-06) |
| Primary citation | Dong, C.,Zhang, H.,Li, L.,Tempel, W.,Loppnau, P.,Min, J. Molecular basis of GID4-mediated recognition of degrons for the Pro/N-end rule pathway. Nat. Chem. Biol., 14:466-473, 2018 Cited by PubMed Abstract: The N-end rule pathway senses the N-terminal destabilizing residues of degradation substrates for the ubiquitin-proteasome system, whose integrity shields against various human syndromes including cancer and cardiovascular diseases. GID4, a subunit of the ubiquitin ligase GID complex, has been recently identified as the N-recognin of the new branch of the N-end rule pathway responsible for recognizing substrates bearing N-terminal proline residues (Pro/N-degrons). However, the molecular mechanism of GID4-mediated Pro/N-degron recognition remains largely unexplored. Here, we report the first crystal structures of human GID4 alone and in complex with various Pro/N-degrons. Our complex crystal structures, together with biophysical analyses, delineate the GID4-mediated Pro/N-degron recognition mechanism and substrate selection criteria for the Pro/N-end rule pathway. These mechanistic data on the Pro/N-recognin activity of GID4 will serve as a foundation to facilitate the identification of authentic physiological substrates as well as the development of inhibitors of therapeutic values for the Pro/N-end rule pathway. PubMed: 29632410DOI: 10.1038/s41589-018-0036-1 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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