1L6N
STRUCTURE OF THE N-TERMINAL 283-RESIDUE FRAGMENT OF THE HIV-1 GAG POLYPROTEIN
Summary for 1L6N
| Entry DOI | 10.2210/pdb1l6n/pdb |
| NMR Information | BMRB: 5316 |
| Descriptor | Gag Polyprotein (1 entity in total) |
| Functional Keywords | gag, matrix, capsid, maturation, viral protein |
| Biological source | Human immunodeficiency virus 1 |
| Cellular location | Matrix protein p17: Virion (By similarity): Q72497 |
| Total number of polymer chains | 1 |
| Total formula weight | 32392.87 |
| Authors | Tang, C.,Ndassa, Y.,Summers, M.F. (deposition date: 2002-03-11, release date: 2002-06-26, Last modification date: 2024-05-22) |
| 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., 9:537-543, 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: 12032547PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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