1a1t
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STRUCTURE OF THE HIV-1 NUCLEOCAPSID PROTEIN BOUND TO THE SL3 PSI-RNA RECOGNITION ELEMENT, NMR, 25 STRUCTURES
OverviewOverview
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.
About this StructureAbout this Structure
1A1T is a Single protein structure of sequence from Human immunodeficiency virus 1 with as ligand. The following page contains interesting information on the relation of 1A1T with [Zinc Fingers]. Full crystallographic information is available from OCA.
ReferenceReference
Structure of the HIV-1 nucleocapsid protein bound to the SL3 psi-RNA recognition element., De Guzman RN, Wu ZR, Stalling CC, Pappalardo L, Borer PN, Summers MF, Science. 1998 Jan 16;279(5349):384-8. PMID:9430589
Page seeded by OCA on Thu Feb 21 11:39:53 2008