7OPO
RSK2 N-terminal kinase domain in complex with ORF45
Summary for 7OPO
| Entry DOI | 10.2210/pdb7opo/pdb |
| Descriptor | Ribosomal protein S6 kinase alpha-3, Protein ORF45, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (4 entities in total) |
| Functional Keywords | orf45, rsk2, rsk, rsk2 ntk, viral modulation, mapkapk, kaposi's sarcoma-associated herpesvirus, viral protein, vf-motif |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 12 |
| Total formula weight | 261221.63 |
| Authors | Sok, P.,Remenyi, A.,Alexa, A.,Poti, A. (deposition date: 2021-06-01, release date: 2022-02-02, Last modification date: 2024-01-31) |
| Primary citation | Alexa, A.,Sok, P.,Gross, F.,Albert, K.,Kobori, E.,Poti, A.L.,Gogl, G.,Bento, I.,Kuang, E.,Taylor, S.S.,Zhu, F.,Ciliberto, A.,Remenyi, A. A non-catalytic herpesviral protein reconfigures ERK-RSK signaling by targeting kinase docking systems in the host. Nat Commun, 13:472-472, 2022 Cited by PubMed Abstract: The Kaposi's sarcoma associated herpesvirus protein ORF45 binds the extracellular signal-regulated kinase (ERK) and the p90 Ribosomal S6 kinase (RSK). ORF45 was shown to be a kinase activator in cells but a kinase inhibitor in vitro, and its effects on the ERK-RSK complex are unknown. Here, we demonstrate that ORF45 binds ERK and RSK using optimized linear binding motifs. The crystal structure of the ORF45-ERK2 complex shows how kinase docking motifs recognize the activated form of ERK. The crystal structure of the ORF45-RSK2 complex reveals an AGC kinase docking system, for which we provide evidence that it is functional in the host. We find that ORF45 manipulates ERK-RSK signaling by favoring the formation of a complex, in which activated kinases are better protected from phosphatases and docking motif-independent RSK substrate phosphorylation is selectively up-regulated. As such, our data suggest that ORF45 interferes with the natural design of kinase docking systems in the host. PubMed: 35078976DOI: 10.1038/s41467-022-28109-x PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.75 Å) |
Structure validation
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