 |
PDBsum entry 1a6b
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Viral protein/DNA
|
PDB id
|
|
|
|
1a6b
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
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.
|
|
|
Authors
|
|
W.Schüler,
C.Dong,
K.Wecker,
B.P.Roques.
|
|
|
Ref.
|
|
Biochemistry, 1999,
38,
12984-12994.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
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 NOE distance restraints, of which 40 were intermolecular, were used
for the structure determination. The zinc finger provides a well-defined surface
for the binding of d(ACGCC) through hydrophobic interactions and tryptophan
stacking on the guanine. This latter interaction was also observed in the
NMR-derived structures of the complexes between NCp7, which contains two
successive zinc fingers, and single-stranded DNA and RNA, supporting the
proposal for a major role played by aromatic residues of NCp proteins in nucleic
acid recognition. Upon binding to the nucleotide a new loop in NCp10 that
participates in the intermolecular interaction is formed. Additional
interactions provided by positively charged residues surrounding the zinc finger
appear necessary for tight binding. The structure of the complex NCp10-d(ACGCC)
gives a structural explanation for the loss of virus infectivity following point
mutations in the finger domain.
|
|
|
Secondary reference #1
|
|
|
Title
|
|
Three-Dimensional 1h nmr structure of the nucleocapsid protein ncp10 of moloney murine leukemia virus.
|
|
|
Authors
|
|
H.Déméné,
N.Jullian,
N.Morellet,
H.De rocquigny,
F.Cornille,
B.Maigret,
B.P.Roques.
|
|
|
Ref.
|
|
J Biomol Nmr, 1994,
4,
153-170.
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
|
|
|
|
