Related ArticlesIdentification of the single-stranded DNA binding surface of the transcriptional coactivator PC4 by NMR.
J Biol Chem. 1999 Feb 5;274(6):3693-9
Authors: Werten S, Wechselberger R, Boelens R, van der Vliet PC, Kaptein R
The C-terminal domain of the eukaryotic transcriptional cofactor PC4 (PC4CTD) is known to bind with nanomolar affinity to single-stranded (ss)DNA. Here, NMR is used to study DNA binding by this domain in more detail. Amide resonance shifts that were observed in a 1H15N-HSQC-monitored titration of 15N-labeled protein with the oligonucleotide dT18 indicate that binding of the nucleic acid occurs by means of two anti-parallel channels that were previously identified in the PC4CTD crystal structure. The beta-sheets and loops that make up these channels exhibit above average flexibility in the absence of ssDNA, which is reflected in higher values of T1rho, reduced heteronuclear nuclear Overhauser effects and faster deuterium exchange rates for the amides in this region. Upon ssDNA binding, this excess flexibility is significantly reduced. The binding of ssDNA by symmetry-related channels reported here provides a structural rationale for the preference of PC4CTD for juxtaposed single-stranded regions (e.g. in heteroduplexes) observed in earlier work.
[NMR paper] Identification of the bile acid-binding site of the ileal lipid-binding protein by ph
Identification of the bile acid-binding site of the ileal lipid-binding protein by photoaffinity labeling, matrix-assisted laser desorption ionization-mass spectrometry, and NMR structure.
Related Articles Identification of the bile acid-binding site of the ileal lipid-binding protein by photoaffinity labeling, matrix-assisted laser desorption ionization-mass spectrometry, and NMR structure.
J Biol Chem. 2001 Mar 9;276(10):7291-301
Authors: Kramer W, Sauber K, Baringhaus KH, Kurz M, Stengelin S, Lange G, Corsiero D, Girbig F, König W, Weyland C
...
nmrlearner
Journal club
0
11-19-2010 08:29 PM
[NMR paper] Identification of the Archaeoglobus fulgidus endonuclease III DNA interaction surface
Identification of the Archaeoglobus fulgidus endonuclease III DNA interaction surface using heteronuclear NMR methods.
Related Articles Identification of the Archaeoglobus fulgidus endonuclease III DNA interaction surface using heteronuclear NMR methods.
Structure. 1999 Aug 15;7(8):919-30
Authors: Shekhtman A, McNaughton L, Cunningham RP, Baxter SM
BACKGROUND: Endonuclease III is the prototype for a family of DNA-repair enzymes that recognize and remove damaged and mismatched bases from DNA via cleavage of the N-glycosidic bond. Crystal...
nmrlearner
Journal club
0
11-18-2010 08:31 PM
[NMR paper] Identification of the DNA binding surface of H-NS protein from Escherichia coli by he
Identification of the DNA binding surface of H-NS protein from Escherichia coli by heteronuclear NMR spectroscopy.
Related Articles Identification of the DNA binding surface of H-NS protein from Escherichia coli by heteronuclear NMR spectroscopy.
FEBS Lett. 1999 Jul 16;455(1-2):63-9
Authors: Shindo H, Ohnuki A, Ginba H, Katoh E, Ueguchi C, Mizuno T, Yamazaki T
The DNA binding domain of H-NS protein was studied with various N-terminal deletion mutant proteins and identified by gel retardation assay and heteronuclear 2D- and 3D-NMR...
nmrlearner
Journal club
0
11-18-2010 08:31 PM
[NMR paper] Identification by NMR of the binding surface for the histidine-containing phosphocarr
Identification by NMR of the binding surface for the histidine-containing phosphocarrier protein HPr on the N-terminal domain of enzyme I of the Escherichia coli phosphotransferase system.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Identification by NMR of the binding surface for the histidine-containing phosphocarrier protein HPr on the N-terminal domain of enzyme I of the Escherichia coli phosphotransferase system.
Biochemistry. 1997 Apr 15;36(15):4393-8
Authors: Garrett DS, Seok YJ,...
nmrlearner
Journal club
0
08-22-2010 03:31 PM
[NMR paper] Identification by NMR of the binding surface for the histidine-containing phosphocarr
Identification by NMR of the binding surface for the histidine-containing phosphocarrier protein HPr on the N-terminal domain of enzyme I of the Escherichia coli phosphotransferase system.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Identification by NMR of the binding surface for the histidine-containing phosphocarrier protein HPr on the N-terminal domain of enzyme I of the Escherichia coli phosphotransferase system.
Biochemistry. 1997 Apr 15;36(15):4393-8
Authors: Garrett DS, Seok YJ,...
nmrlearner
Journal club
0
08-22-2010 03:03 PM
[NMR paper] Comparison of Pf1 and Fd gene 5 proteins and their single-stranded DNA complexes by N
Comparison of Pf1 and Fd gene 5 proteins and their single-stranded DNA complexes by NMR spectroscopy and differential scanning calorimetry.
Related Articles Comparison of Pf1 and Fd gene 5 proteins and their single-stranded DNA complexes by NMR spectroscopy and differential scanning calorimetry.
Biochemistry. 1995 Jan 10;34(1):148-54
Authors: Davis KG, Plyte SE, Robertson SR, Cooper A, Kneale GG
The Pf1 gene 5 protein forms a large helical nucleoprotein complex (Mr = 3.1 x 10(7)) with single-stranded viral DNA, from which a 32 amino acid...
nmrlearner
Journal club
0
08-22-2010 03:41 AM
[NMR paper] Secondary structure of the single-stranded DNA binding protein encoded by filamentous
Secondary structure of the single-stranded DNA binding protein encoded by filamentous phage Pf3 as determined by NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Secondary structure of the single-stranded DNA binding protein encoded by filamentous phage Pf3 as determined by NMR.
Eur J Biochem. 1994 Sep 1;224(2):663-76
Authors: Folmer RH, Folkers PJ, Kaan A, Jonker AJ, Aelen JM, Konings RN, Hilbers CW
Nuclear magnetic resonance...
nmrlearner
Journal club
0
08-22-2010 03:29 AM
[NMR paper] The identification of cation-binding domains on the surface of microsomal cytochrome
The identification of cation-binding domains on the surface of microsomal cytochrome b5 using 1H-NMR paramagnetic difference spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles The identification of cation-binding domains on the surface of microsomal cytochrome b5 using 1H-NMR paramagnetic difference spectroscopy.
Eur J Biochem. 1992 Jan 15;203(1-2):211-23
Authors: Whitford D
One-dimensional and two-dimensional 1H-NMR...
Identification of the single-stranded DNA binding surface of the transcriptional coac
Linear Mode
