1A6S
M-DOMAIN FROM GAG POLYPROTEIN OF ROUS SARCOMA VIRUS, NMR, 20 STRUCTURES
Summary for 1A6S
| Entry DOI | 10.2210/pdb1a6s/pdb |
| Descriptor | GAG POLYPROTEIN (1 entity in total) |
| Functional Keywords | core protein, virus structure, membrane binding, viral protein |
| Biological source | Rous sarcoma virus - Prague C |
| Cellular location | Matrix protein p19: Virion (Potential). Capsid protein p27: Virion (Potential). Nucleocapsid protein p12: Virion (Potential): P03322 |
| Total number of polymer chains | 1 |
| Total formula weight | 9179.75 |
| Authors | Mcdonnell, J.M.,Fushman, D.,Cahill, S.M.,Zhou, W.,Wolven, A.,Wilson, C.B.,Nelle, T.D.,Resh, M.D.,Wills, J.,Cowburn, D. (deposition date: 1998-03-02, release date: 1998-10-14, Last modification date: 2024-05-22) |
| Primary citation | McDonnell, J.M.,Fushman, D.,Cahill, S.M.,Zhou, W.,Wolven, A.,Wilson, C.B.,Nelle, T.D.,Resh, M.D.,Wills, J.,Cowburn, D. Solution structure and dynamics of the bioactive retroviral M domain from Rous sarcoma virus J.Mol.Biol., 279:921-928, 1998 Cited by PubMed Abstract: A biologically active construct of the retroviral M domain from the avian Rous sarcoma virus is defined and its solution structure described. This M domain is fully active in budding and infectivity without myristylation. In spite of a sequence homology level that suggests no relationship among M domains and the family of matrix proteins in mammalian retroviruses, the conserved structural elements of a central core allow an M domain sequence motif to be described for all retroviruses. The surface of the M domain has a highly clustered positive patch comprised of sequentially distant residues. An analysis of the backbone dynamics, incorporating rotational anisotropy, is used to estimate the thermodynamics of proposed domain oligomerization. PubMed: 9642071DOI: 10.1006/jmbi.1998.1788 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
