TY - JOUR
T1 - Structure of the HIV-1 nucleocapsid protein bound to the SL3 ψ-RNA recognition element
AU - De Guzman, Roberto N.
AU - Wu, Zheng Rong
AU - Stalling, Chelsea C.
AU - Pappalardo, Lucia
AU - Borer, Philip N.
AU - Summers, Michael F.
PY - 1998/1/16
Y1 - 1998/1/16
N2 - 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 Ψ RNA packaging signal has been determined by heteronuclear magnetic resonance spectroscopy. Tight binding (dissociation constant, ~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.
AB - 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 Ψ RNA packaging signal has been determined by heteronuclear magnetic resonance spectroscopy. Tight binding (dissociation constant, ~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.
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U2 - 10.1126/science.279.5349.384
DO - 10.1126/science.279.5349.384
M3 - Article
C2 - 9430589
AN - SCOPUS:2242469712
SN - 0036-8075
VL - 279
SP - 384
EP - 388
JO - Science
JF - Science
IS - 5349
ER -