Summary information and primary citation
- PDB-id
-
1a1t;
SNAP-derived features in text and
JSON formats
- Class
- viral protein-RNA
- Method
- NMR
- Summary
- Structure of the hiv-1 nucleocapsid protein bound to
the sl3 psi-RNA recognition element, NMR, 25
structures
- Reference
-
De Guzman RN, Wu ZR, Stalling CC, Pappalardo L, Borer PN,
Summers MF (1998): "Structure
of the HIV-1 nucleocapsid protein bound to the SL3
psi-RNA recognition element." Science,
279, 384-388. doi: 10.1126/science.279.5349.384.
- Abstract
- The three-dimensional structure of the human
immunodeficiency virus-type 1 (HIV-1) nucleocapsid protein
(NC) bound to the SL3 stem-loop recognition element of the
genomic Psi RNA packaging signal has been determined by
heteronuclear magnetic resonance spectroscopy. Tight
binding (dissociation constant, approximately 100 nM) is
mediated by specific interactions between the amino- and
carboxyl-terminal CCHC-type zinc knuckles of the NC protein
and the G7 and G9 nucleotide bases, respectively, of the
G6-G7-A8-G9 RNA tetraloop. A8 packs against the
amino-terminal knuckle and forms a hydrogen bond with
conserved Arg32, and residues Lys3 to Arg10 of NC form a
310 helix that binds to the major groove of the RNA stem
and also packs against the amino-terminal zinc knuckle. The
structure provides insights into the mechanism of viral
genome recognition, explains extensive amino acid
conservation within NC, and serves as a basis for the
development of inhibitors designed to interfere with genome
encapsidation.
