4IPY
HIV capsid C-terminal domain
Summary for 4IPY
| Entry DOI | 10.2210/pdb4ipy/pdb |
| Related | 1A8O |
| Descriptor | Capsid protein p24, 1,2-ETHANEDIOL (3 entities in total) |
| Functional Keywords | viral protein, capsid, core protein |
| Biological source | Human immunodeficiency virus type 1 (HIV-1) |
| Cellular location | Gag-Pol polyprotein: Host cell membrane; Lipid-anchor . Matrix protein p17: Virion membrane; Lipid- anchor . Capsid protein p24: Virion . Nucleocapsid protein p7: Virion . Reverse transcriptase/ribonuclease H: Virion . Integrase: Virion : P12497 |
| Total number of polymer chains | 4 |
| Total formula weight | 38710.53 |
| Authors | Lampel, A.,Yaniv, O.,Berger, O.,Bachrach, E.,Gazit, E.,Frolow, F. (deposition date: 2013-01-10, release date: 2013-10-16, Last modification date: 2024-10-30) |
| Primary citation | Lampel, A.,Yaniv, O.,Berger, O.,Bacharach, E.,Gazit, E.,Frolow, F. A triclinic crystal structure of the carboxy-terminal domain of HIV-1 capsid protein with four molecules in the asymmetric unit reveals a novel packing interface. Acta Crystallogr.,Sect.F, 69:602-606, 2013 Cited by PubMed Abstract: The Gag precursor is the major structural protein of the virion of human immunodeficiency virus-1 (HIV-1). Capsid protein (CA), a cleavage product of Gag, plays an essential role in virus assembly both in Gag-precursor multimerization and in capsid core formation. The carboxy-terminal domain (CTD) of CA contains 20 residues that are highly conserved across retroviruses and constitute the major homology region (MHR). Genetic evidence implies a role for the MHR in interactions between Gag precursors during the assembly of the virus, but the structural basis for this role remains elusive. This paper describes a novel triclinic structure of the HIV-1 CA CTD at 1.6 Å resolution with two canonical dimers of CA CTD in the asymmetric unit. The canonical dimers form a newly identified packing interface where interactions of four conserved MHR residues take place. This is the first structural indication that these MHR residues participate in the putative CTD-CTD interactions. These findings suggest that the molecules forming this novel interface resemble an intermediate structure that participates in the early steps of HIV-1 assembly. This interface may therefore provide a novel target for antiviral drugs. PubMed: 23722834DOI: 10.1107/S1744309113011871 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.64 Å) |
Structure validation
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