4O46
14-3-3-gamma in complex with influenza NS1 C-terminal tail phosphorylated at S228
Summary for 4O46
Entry DOI | 10.2210/pdb4o46/pdb |
Descriptor | 14-3-3 protein gamma, Nonstructural protein 1, Unidentified polymer, ... (4 entities in total) |
Functional Keywords | viral protein, influenza, structural genomics, structural genomics consortium, sgc |
Biological source | Homo sapiens (human) More |
Cellular location | Cytoplasm (By similarity): P61981 Host nucleus: Q9YP60 |
Total number of polymer chains | 16 |
Total formula weight | 196444.19 |
Authors | Qin, S.,Liu, Y.,Tempel, W.,Arrowsmith, C.H.,Bountra, C.,Edwards, A.M.,Min, J.,Structural Genomics Consortium (SGC) (deposition date: 2013-12-18, release date: 2014-04-30, Last modification date: 2024-10-30) |
Primary citation | Qin, S.,Liu, Y.,Tempel, W.,Eram, M.S.,Bian, C.,Liu, K.,Senisterra, G.,Crombet, L.,Vedadi, M.,Min, J. Structural basis for histone mimicry and hijacking of host proteins by influenza virus protein NS1. Nat Commun, 5:3952-3952, 2014 Cited by PubMed Abstract: Pathogens can interfere with vital biological processes of their host by mimicking host proteins. The NS1 protein of the influenza A H3N2 subtype possesses a histone H3K4-like sequence at its carboxyl terminus and has been reported to use this mimic to hijack host proteins. However, this mimic lacks a free N-terminus that is essential for binding to many known H3K4 readers. Here we show that the double chromodomains of CHD1 adopt an 'open pocket' to interact with the free N-terminal amine of H3K4, and the open pocket permits the NS1 mimic to bind in a distinct conformation. We also explored the possibility that NS1 hijacks other cellular proteins and found that the NS1 mimic has access to only a subset of chromatin-associated factors, such as WDR5. Moreover, methylation of the NS1 mimic can not be reversed by the H3K4 demethylase LSD1. Overall, we thus conclude that the NS1 mimic is an imperfect histone mimic. PubMed: 24853335DOI: 10.1038/ncomms4952 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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