7RGW
Crystal structure of HERC2 DOC domain
Summary for 7RGW
| Entry DOI | 10.2210/pdb7rgw/pdb |
| Descriptor | E3 ubiquitin-protein ligase HERC2, DI(HYDROXYETHYL)ETHER (3 entities in total) |
| Functional Keywords | doc domain of e3 ubiquitin ligase herc2, cell cycle |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 19694.58 |
| Authors | Liu, J.,Tencer, A.H.,Kutateladze, T.G. (deposition date: 2021-07-15, release date: 2022-07-20, Last modification date: 2023-10-25) |
| Primary citation | Tencer, A.H.,Liu, J.,Zhu, J.,Burkholder, N.T.,Zhang, Y.,Wu, W.,Strahl, B.D.,Ohta, T.,Kutateladze, T.G. The ZZ domain of HERC2 is a receptor of arginylated substrates. Sci Rep, 12:6063-6063, 2022 Cited by PubMed Abstract: The E3 ubiquitin ligase HERC2 has been linked to neurological diseases and cancer, however it remains a poorly characterized human protein. Here, we show that the ZZ domain of HERC2 (HERC2) recognizes a mimetic of the Nt-R cargo degradation signal. NMR titration experiments and mutagenesis results reveal that the Nt-R mimetic peptide occupies a well-defined binding site of HERC2 comprising of the negatively charged aspartic acids. We report the crystal structure of the DOC domain of HERC2 (HERC2) that is adjacent to HERC2 and show that a conformational rearrangement in the protein may occur when the two domains are linked. Immunofluorescence microscopy data suggest that the stimulation of autophagy promotes targeting of HERC2 to the proteasome. Our findings suggest a role of cytosolic HERC2 in the ubiquitin-dependent degradation pathways. PubMed: 35411094DOI: 10.1038/s41598-022-10119-w PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.99 Å) |
Structure validation
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