Related ArticlesStructure of the His44 --> Ala single point mutant of the distal finger motif of HIV-1 nucleocapsid protein: a combined NMR, molecular dynamics simulation, and fluorescence study.
Biochemistry. 2004 Jun 22;43(24):7687-97
Authors: Stote RH, Kellenberger E, Muller H, Bombarda E, Roques BP, Kieffer B, Mély Y
The nucleocapsid protein (NCp7) of human immunodeficiency virus type 1 (HIV-1) contains two highly conserved CCHC zinc fingers that strongly bind Zn(2+) through coordination of one His and three Cys residues. It has been suggested that NCp7 function is conformation specific since substitution of any of the zinc coordinating residues in the zinc finger motifs leads to subsequent loss of viral infectivity. To further determine the structural requirements necessary for this specific conformation, we investigated by (1)H 2D NMR and molecular dynamics simulations the structure of the distal finger motif of NCp7 in which the zinc coordinating amino acid, His 44, was substituted by a noncoordinating Ala residue. While the fold of the N-terminal part of this mutated peptide was similar to that of the native peptide, an increased lability and significant conformational changes were observed in the vicinity of the His-to-Ala mutation. Moreover, molecular dynamics simulations suggested a mechanism by which the variant peptide can bind zinc ion even though one zinc-coordinating amino acid was lacking. Using the fluorescence of the naturally occurring Trp37 residue, the binding affinity of the variant peptide to the (TG)(3) model oligonucleotide was found to be decreased by about 2 orders of magnitude with respect with the native peptide. Modeling of the DNA:NCp7 complex using structures of the variant peptide suggests that the residues forming a hydrophobic cleft in the native protein are improperly oriented for efficient DNA binding by the variant peptide.
[NMR paper] NMR structure of the first PHD finger of autoimmune regulator protein (AIRE1). Insigh
NMR structure of the first PHD finger of autoimmune regulator protein (AIRE1). Insights into autoimmune polyendocrinopathy-candidiasis-ectodermal dystrophy (APECED) disease.
Related Articles NMR structure of the first PHD finger of autoimmune regulator protein (AIRE1). Insights into autoimmune polyendocrinopathy-candidiasis-ectodermal dystrophy (APECED) disease.
J Biol Chem. 2005 Mar 25;280(12):11505-12
Authors: Bottomley MJ, Stier G, Pennacchini D, Legube G, Simon B, Akhtar A, Sattler M, Musco G
Mutations in the autoimmune regulator protein...
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11-24-2010 11:14 PM
[NMR paper] NMR structure of the single QALGGH zinc finger domain from the Arabidopsis thaliana S
NMR structure of the single QALGGH zinc finger domain from the Arabidopsis thaliana SUPERMAN protein.
Related Articles NMR structure of the single QALGGH zinc finger domain from the Arabidopsis thaliana SUPERMAN protein.
Chembiochem. 2003 Mar 3;4(2-3):171-80
Authors: Isernia C, Bucci E, Leone M, Zaccaro L, Di Lello P, Digilio G, Esposito S, Saviano M, Di Blasio B, Pedone C, Pedone PV, Fattorusso R
Zinc finger domains of the classical type represent the most abundant DNA binding domains in eukaryotic transcription factors. Plant proteins...
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[NMR paper] NMR studies of metal ion binding to the Zn-finger-like HNH motif of colicin E9.
NMR studies of metal ion binding to the Zn-finger-like HNH motif of colicin E9.
Related Articles NMR studies of metal ion binding to the Zn-finger-like HNH motif of colicin E9.
J Inorg Biochem. 2000 Apr;79(1-4):365-70
Authors: Hannan JP, Whittaker SB, Hemmings AM, James R, Kleanthous C, Moore GR
The 134 amino acid DNase domain of colicin E9 contains a zinc-finger-like HNH motif that binds divalent transition metal ions. We have used 1D 1H and 2D 1H-15N NMR methods to characterise the binding of Co2+, Ni2+ and Zn2+ to this protein. Data for the...
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[NMR paper] NMR characterization of a single-cysteine mutant of Escherichia coli thioredoxin and
NMR characterization of a single-cysteine mutant of Escherichia coli thioredoxin and a covalent thioredoxin-peptide complex.
Related Articles NMR characterization of a single-cysteine mutant of Escherichia coli thioredoxin and a covalent thioredoxin-peptide complex.
Eur J Biochem. 1998 Oct 15;257(2):299-308
Authors: Jeng MF, Reymond MT, Tennant LL, Holmgren A, Dyson HJ
The mechanism of disulfide reduction by thioredoxin in the cell is thought to occur through the formation and subsequent destruction of a mixed-disulfide intermediate between...
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[NMR paper] NMR structure and dynamics of an RNA motif common to the spliceosome branch-point hel
NMR structure and dynamics of an RNA motif common to the spliceosome branch-point helix and the RNA-binding site for phage GA coat protein.
Related Articles NMR structure and dynamics of an RNA motif common to the spliceosome branch-point helix and the RNA-binding site for phage GA coat protein.
Biochemistry. 1998 Sep 29;37(39):13486-98
Authors: Smith JS, Nikonowicz EP
The RNA molecules that make up the spliceosome branch-point helix and the binding site for phage GA coat protein share a secondary structure motif in which two consecutive...
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[NMR paper] Two-dimensional NMR studies of the zinc finger motif: solution structures and dynamic
Two-dimensional NMR studies of the zinc finger motif: solution structures and dynamics of mutant ZFY domains containing aromatic substitutions in the hydrophobic core.
Related Articles Two-dimensional NMR studies of the zinc finger motif: solution structures and dynamics of mutant ZFY domains containing aromatic substitutions in the hydrophobic core.
Biochemistry. 1992 Aug 25;31(33):7463-76
Authors: Qian X, Weiss MA
Solution structures of mutant Zn fingers containing aromatic substitutions in the hydrophobic core are determined by 2D-NMR...
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[NMR paper] Architectural rules of the zinc-finger motif: comparative two-dimensional NMR studies
Architectural rules of the zinc-finger motif: comparative two-dimensional NMR studies of native and "aromatic-swap" domains define a "weakly polar switch".
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Architectural rules of the zinc-finger motif: comparative two-dimensional NMR studies of native and "aromatic-swap" domains define a "weakly polar switch".
Proc Natl Acad Sci U S A. 1991 Oct 1;88(19):8455-9
Authors: Kochoyan M, Keutmann HT, Weiss MA
The...
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[NMR paper] Architectural rules of the zinc-finger motif: comparative two-dimensional NMR studies
Architectural rules of the zinc-finger motif: comparative two-dimensional NMR studies of native and "aromatic-swap" domains define a "weakly polar switch".
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Architectural rules of the zinc-finger motif: comparative two-dimensional NMR studies of native and "aromatic-swap" domains define a "weakly polar switch".
Proc Natl Acad Sci U S A. 1991 Oct 1;88(19):8455-9
Authors: Kochoyan M, Keutmann HT, Weiss MA
The...