4ZV5
Crystal structure of N-myristoylated mouse mammary tumor virus matrix protein
Summary for 4ZV5
| Entry DOI | 10.2210/pdb4zv5/pdb |
| Descriptor | Matrix protein p10, MYRISTIC ACID (3 entities in total) |
| Functional Keywords | retroviral matrix protein, n-myristoylation, viral protein |
| Biological source | Mouse mammary tumor virus (MMTV) |
| Cellular location | Matrix protein p10: Virion . Capsid protein p27: Virion . Nucleocapsid protein p14: Virion : P10258 |
| Total number of polymer chains | 2 |
| Total formula weight | 21434.85 |
| Authors | Zabransky, A.,Dolezal, M.,Dostal, J.,Vanek, O.,Hadravova, R.,Stokrova, J.,Brynda, J.,Pichova, I. (deposition date: 2015-05-18, release date: 2016-01-27, Last modification date: 2024-11-13) |
| Primary citation | Dolezal, M.,Zabransky, A.,Dostal, J.,Vanek, O.,Brynda, J.,Lepsik, M.,Hadravova, R.,Pichova, I. Myristoylation drives dimerization of matrix protein from mouse mammary tumor virus. Retrovirology, 13:2-2, 2016 Cited by PubMed Abstract: Myristoylation of the matrix (MA) domain mediates the transport and binding of Gag polyproteins to the plasma membrane (PM) and is required for the assembly of most retroviruses. In betaretroviruses, which assemble immature particles in the cytoplasm, myristoylation is dispensable for assembly but is crucial for particle transport to the PM. Oligomerization of HIV-1 MA stimulates the transition of the myristoyl group from a sequestered to an exposed conformation, which is more accessible for membrane binding. However, for other retroviruses, the effect of MA oligomerization on myristoyl group exposure has not been thoroughly investigated. PubMed: 26728401DOI: 10.1186/s12977-015-0235-8 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.57 Å) |
Structure validation
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