1a6b
NMR STRUCTURE OF THE COMPLEX BETWEEN THE ZINC FINGER PROTEIN NCP10 OF MOLONEY MURINE LEUKEMIA VIRUS AND A SEQUENCE OF THE PSI-PACKAGING DOMAIN OF HIV-1, 20 STRUCTURES
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OverviewOverview
The structure of the 56 amino acid nucleocapsid protein NCp10 of, retrovirus MoMuLV, which contains a single CX(2)CX(4)HX(4)C-type zinc, finger, has been determined previously by NMR. The important role of NCp10, (or NCp7 for HIV-1) in the retroviral life cycle seems mainly related to, their preferential binding to single-stranded nucleic acids. We report, here the structure of the complex formed between the biologically active, (14-53)NCp10 and the oligonucleotide d(ACGCC) in aqueous solution, determined by 2D (1)H NMR based methods. The aromatic residue Trp(35) of, NCp10 directs nucleic acid complexation as shown by its complete, fluorescence quenching upon addition of d(ACGCC). (1)H and (31)P NMR, studies support the insertion of Trp(35) between the G(3) and C(4) bases., A total of 577 ... [(full description)]
About this StructureAbout this Structure
1A6B is a [Single protein] structure of sequence from [[1]] with ZN as [ligand]. Full crystallographic information is available from [OCA].
ReferenceReference
NMR structure of the complex between the zinc finger protein NCp10 of Moloney murine leukemia virus and the single-stranded pentanucleotide d(ACGCC): comparison with HIV-NCp7 complexes., Schuler W, Dong C, Wecker K, Roques BP, Biochemistry. 1999 Oct 5;38(40):12984-94. PMID:10529168
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