6NHJ
Atomic structures and deletion mutant reveal different capsid-binding patterns and functional significance of tegument protein pp150 in murine and human cytomegaloviruses with implications for therapeutic development
This is a non-PDB format compatible entry.
Summary for 6NHJ
Entry DOI | 10.2210/pdb6nhj/pdb |
EMDB information | 9366 9367 9368 9369 |
Descriptor | Major capsid protein, Tegument protein, Small capsomere-interacting protein, ... (5 entities in total) |
Functional Keywords | cryoem, beta-herpesvirus, murine cytomegalovirus, human cytomegalovirus, pp150, pul32, pm32, bacterial artificial chromosome-based mutagenesis, virus |
Biological source | Murine cytomegalovirus (strain Smith) (MuHV-1) More |
Total number of polymer chains | 55 |
Total formula weight | 3727300.42 |
Authors | Liu, W.,Dai, X.H.,Jih, J.,Chan, K.,Trang, P.,Yu, X.K.,Balogun, R.,Mei, Y.,Liu, F.Y.,Zhou, Z.H. (deposition date: 2018-12-22, release date: 2019-03-06, Last modification date: 2019-11-27) |
Primary citation | Liu, W.,Dai, X.,Jih, J.,Chan, K.,Trang, P.,Yu, X.,Balogun, R.,Mei, Y.,Liu, F.,Zhou, Z.H. Atomic structures and deletion mutant reveal different capsid-binding patterns and functional significance of tegument protein pp150 in murine and human cytomegaloviruses with implications for therapeutic development. PLoS Pathog., 15:e1007615-e1007615, 2019 Cited by PubMed: 30779794DOI: 10.1371/journal.ppat.1007615 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (5 Å) |
Structure validation
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