1Q3Z
NMR structure of the Cys28His mutant (E form) of the nucleocapsid protein NCp7 of HIV-1.
Summary for 1Q3Z
| Entry DOI | 10.2210/pdb1q3z/pdb |
| Related | 1ESK 1Q3Y |
| Descriptor | GAG protein, ZINC ION (2 entities in total) |
| Functional Keywords | cchc zinc knuckle, cchh zinc knuckle, viral protein |
| Total number of polymer chains | 1 |
| Total formula weight | 5003.46 |
| Authors | Ramboarina, S.,Druillennec, S.,Morellet, N.,Bouaziz, S.,Roques, B.P. (deposition date: 2003-08-01, release date: 2004-09-07, Last modification date: 2024-05-22) |
| Primary citation | Ramboarina, S.,Druillennec, S.,Morellet, N.,Bouaziz, S.,Roques, B.P. Target specificity of human immunodeficiency virus type 1 NCp7 requires an intact conformation of its CCHC N-terminal zinc finger. J.Virol., 78:6682-6687, 2004 Cited by PubMed Abstract: The modification of zinc-binding residues inside the conserved CCHC motif of human immunodeficiency virus type 1 NCp7, in particular into CCHH, induces a complete loss of infectivity. Since the mutant His28NCp7 has been shown to be devoid of infectivity in vivo, the structure-function relationships of the mutant His28(12-53)NCp7 were investigated by nuclear magnetic resonance and surface plasmonic resonance. Although the Cys28-->His mutation modifies drastically the structure of the core domain (residues 12 to 53) of NCp7, His28(12-53)NCp7 still interacts with a 10-fold-lower affinity to specific nucleic acid targets, such as SL3, a stem-loop critically involved in viral RNA packaging, and without affinity change with the nonspecific, single-stranded nucleic acid poly(T). Moreover, His28(12-53)NCp7 and native (12-53)NCp7 displayed the same affinity with reverse transcriptase, but the natures of the complexes are probably different, accounting for the drastic reduction in the amount of RNA packaged in the mutated virus. We propose a structural model of His28(12-53)NCp7 that provides insights into the NCp7 structural features necessary for target recognition and that shows that the specific native structure of the zinc finger domain is strictly required for the optimal target selectivity of NCp7. PubMed: 15163759DOI: 10.1128/JVI.78.12.6682-6687.2004 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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