Summary for 1BAX
| Entry DOI | 10.2210/pdb1bax/pdb |
| Descriptor | M-PMV MATRIX PROTEIN (1 entity in total) |
| Functional Keywords | matrix protein, core protein, polyprotein, myristylation |
| Biological source | Mason-Pfizer monkey virus |
| Cellular location | Matrix protein p10: Virion (Potential). Capsid protein p27: Virion (Potential). Nucleocapsid protein p14: Virion (Potential): P07567 |
| Total number of polymer chains | 1 |
| Total formula weight | 11316.98 |
| Authors | Conte, M.R.,Klikova, M.,Hunter, E.,Ruml, T.,Matthews, S. (deposition date: 1998-04-20, release date: 1998-06-17, Last modification date: 2024-04-10) |
| Primary citation | Conte, M.R.,Klikova, M.,Hunter, E.,Ruml, T.,Matthews, S. The three-dimensional solution structure of the matrix protein from the type D retrovirus, the Mason-Pfizer monkey virus, and implications for the morphology of retroviral assembly. EMBO J., 16:5819-5826, 1997 Cited by PubMed Abstract: The Mason-Pfizer monkey virus (M-PMV) is the prototype of the type D retroviruses. In type B and D retroviruses, the Gag protein pre-assembles before association with the membrane, whereas in type C retroviruses (lentiviruses, BLV/HTLV group) Gag is targeted efficiently to the plasma membrane, where the particle formation occurs. The N-terminal domain of Gag, the matrix protein (MA), plays a critical role in determining this morphogenic difference. We have determined the three-dimensional solution structure of the M-PMV MA by heteronuclear nuclear magnetic resonance. The protein contains four alpha-helices that are structurally similar to the known type C MA structures. This similarity implies possible common assembly units and membrane-binding mechanisms for type C and B/D retroviruses. In addition to this, the interpretation of mutagenesis data has enabled us to identify, for the first time, the structural basis of a putative intracellular targeting motif. PubMed: 9312040DOI: 10.1093/emboj/16.19.5819 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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