2F76
Solution structure of the M-PMV wild type matrix protein (p10)
Summary for 2F76
| Entry DOI | 10.2210/pdb2f76/pdb |
| Related | 2F77 |
| NMR Information | BMRB: 6400 |
| Descriptor | Core protein p10 (1 entity in total) |
| Functional Keywords | 4 alpha-helices, viral protein |
| Biological source | Simian retrovirus 1 |
| Cellular location | Matrix protein p10: Virion (Potential). Capsid protein p27: Virion (Potential). Nucleocapsid protein p14: Virion (Potential): P04022 |
| Total number of polymer chains | 1 |
| Total formula weight | 11985.78 |
| Authors | Vlach, J.,Lipov, J.,Veverka, V.,Lang, J.,Srb, P.,Rumlova, M.,Hunter, E.,Ruml, T.,Hrabal, R. (deposition date: 2005-11-30, release date: 2006-12-05, Last modification date: 2024-05-29) |
| Primary citation | Vlach, J.,Lipov, J.,Rumlova, M.,Veverka, V.,Lang, J.,Srb, P.,Knejzlik, Z.,Pichova, I.,Hunter, E.,Hrabal, R.,Ruml, T. D-retrovirus morphogenetic switch driven by the targeting signal accessibility to Tctex-1 of dynein. Proc.Natl.Acad.Sci.USA, 105:10565-10570, 2008 Cited by PubMed Abstract: Despite extensive data demonstrating that immature retroviral particle assembly can take place either at the plasma membrane or at a distinct location within the cytoplasm, targeting of viral precursor proteins to either assembly site still remains poorly understood. Biochemical data presented here suggest that Tctex-1, a light chain of the molecular motor dynein, is involved in the intracellular targeting of Mason-Pfizer monkey virus (M-PMV) polyproteins to the cytoplasmic assembly site. Comparison of the three-dimensional structures of M-PMV wild-type matrix protein (wt MA) with a single amino acid mutant (R55F), which redirects assembly from a cytoplasmic site to the plasma membrane, revealed different mutual orientations of their C- and N-terminal domains. This conformational change buries a putative intracellular targeting motif located between both domains in the hydrophobic pocket of the MA molecule, thereby preventing the interaction with cellular transport mechanisms. PubMed: 18647839DOI: 10.1073/pnas.0801765105 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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