1GWP
STRUCTURE OF THE N-TERMINAL DOMAIN OF THE MATURE HIV-1 CAPSID PROTEIN
Replaces: 1GDSReplaces: 1GDYReplaces: 1GDZSummary for 1GWP
| Entry DOI | 10.2210/pdb1gwp/pdb |
| Related | 1A43 1A8O 1AFV 1AK4 1AUM 1BAJ 1HIW 2HMX |
| Descriptor | GAG POLYPROTEIN (1 entity in total) |
| Functional Keywords | human immunodeficiency virus type 1 capsid protein, amimo-terminal core domain, hiv-1 ca-151, virus capsid protein, virus maturation, viral protein |
| Biological source | HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 (NEW YORK-5 ISOLATE) |
| Cellular location | Matrix protein p17: Virion (Potential). Capsid protein p24: Virion (Potential). Nucleocapsid protein p7: Virion (Potential): P12493 |
| Total number of polymer chains | 1 |
| Total formula weight | 16716.19 |
| Authors | Tang, C.,Gitti, R.K.,Lee, B.M.,Walker, J.,Summers, M.F.,Yoo, S.,Sundquist, W.I. (deposition date: 2002-03-22, release date: 2002-06-21, Last modification date: 2024-05-15) |
| Primary citation | Tang, C.,Ndassa, Y.,Summers, M.F. Structure of the N-Terminal 283-Residue Fragment of the Immature HIV-1 Gag Polyprotein Nat.Struct.Biol., 9:537-, 2002 Cited by PubMed Abstract: The capsid protein (CA) of the mature human immunodeficiency virus (HIV) contains an N-terminal beta-hairpin that is essential for formation of the capsid core particle. CA is generated by proteolytic cleavage of the Gag precursor polyprotein during viral maturation. We have determined the NMR structure of a 283-residue N-terminal fragment of immature HIV-1 Gag (Gag(283)), which includes the intact matrix (MA) and N-terminal capsid (CA(N)) domains. The beta-hairpin is unfolded in Gag(283), consistent with the proposal that hairpin formation occurs subsequent to proteolytic cleavage of Gag, triggering capsid assembly. Comparison of the immature and mature CA(N) structures reveals that beta-hairpin formation induces a approximately 2 A displacement of helix 6 and a concomitant displacement of the cyclophylin-A (CypA)-binding loop, suggesting a possible allosteric mechanism for CypA-mediated destabilization of the capsid particle during infectivity. PubMed: 12032547DOI: 10.1038/NSB806 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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