Related ArticlesNMR spectroscopy reveals the solution dimerization interface of p53 core domains bound to their consensus DNA.
J Biol Chem. 2001 Dec 28;276(52):49020-7
Authors: Klein C, Planker E, Diercks T, Kessler H, Künkele KP, Lang K, Hansen S, Schwaiger M
The p53 protein is a transcription factor that acts as the major tumor suppressor in mammals. The core DNA-binding domain is mutated in about 50% of all human tumors. The crystal structure of the core domain in complex with DNA illustrated how a single core domain specifically interacts with its DNA consensus site and how it is inactivated by mutation. However, no structural information for the tetrameric full-length p53-DNA complex is available. Here, we present novel experimental insight into the dimerization of two p53 core domains upon cooperative binding to consensus DNA in solution obtained by NMR. The NMR data show that the p53 core domain itself does not appear to undergo major conformational changes upon addition of DNA and elucidate the dimerization interface between two DNA-bound core domains, which includes the short H1 helix. A NMR-based model for the dimeric p53 core-DNA complex incorporates these data and allows the conclusion that the dimerization interface also forms the actual interface in the tetrameric p53-DNA complex. The significance of this interface is further corroborated by the finding that hot spot mutations map to the H1 helix, and by the binding of the putative p53 inhibitor 53BP2 to this region via one of its ankyrin repeats. Based on symmetry considerations it is proposed that tetrameric p53 might link non-contiguous DNA consensus sites in a sandwich-like manner generating DNA loops as observed for transcriptionally active p53 complexes.
NMR study of the structure and self-association of Core peptide in aqueous solution and DPC micelles.
NMR study of the structure and self-association of Core peptide in aqueous solution and DPC micelles.
NMR study of the structure and self-association of Core peptide in aqueous solution and DPC micelles.
Biopolymers. 2011;96(2):177-80
Authors: Zheng G, Torres AM, Ali M, Manolios N, Price WS
Core peptide is a hydrophobic peptide derived from the T-cell antigen receptor-alpha chain (TCR-alpha) transmembrane region with therapeutic potential. The mechanism by which the peptide inserts into the membrane, including any requirements to change...
nmrlearner
Journal club
0
07-20-2011 10:00 AM
Solution structure, dynamics and thermodynamics of the three SH3 domains of CD2AP
Solution structure, dynamics and thermodynamics of the three SH3 domains of CD2AP
Abstract CD2 associated protein (CD2AP) is an adaptor protein that plays an important role in cell to cell union needed for the kidney function. It contains three N-terminal SH3 domains that are able to interact among others with CD2, ALIX, c-Cbl and Ubiquitin. To understand the role of the individual SH3 domains of this adaptor protein we have performed a complete structural, thermodynamic and dynamic characterization of the separate domains using NMR and DSC. The energetic contributions to the stability...
nmrlearner
Journal club
0
05-01-2011 04:48 AM
[NMR paper] Solution structure of the two N-terminal RNA-binding domains of nucleolin and NMR stu
Solution structure of the two N-terminal RNA-binding domains of nucleolin and NMR study of the interaction with its RNA target.
Related Articles Solution structure of the two N-terminal RNA-binding domains of nucleolin and NMR study of the interaction with its RNA target.
J Mol Biol. 2000 Oct 20;303(2):227-41
Authors: Allain FH, Gilbert DE, Bouvet P, Feigon J
Nucleolin is an abundant 70 kDa nucleolar protein involved in many aspects of ribosomal RNA biogenesis. The central region of nucleolin contains four tandem consensus RNA-binding domains...
nmrlearner
Journal club
0
11-19-2010 08:29 PM
[NMR paper] An automated approach for defining core atoms and domains in an ensemble of NMR-deriv
An automated approach for defining core atoms and domains in an ensemble of NMR-derived protein structures.
Related Articles An automated approach for defining core atoms and domains in an ensemble of NMR-derived protein structures.
Protein Eng. 1997 Jun;10(6):737-41
Authors: Kelley LA, Gardner SP, Sutcliffe MJ
A single NMR-derived protein structure is usually deposited as an ensemble containing many structures, each consistent with the restraint set used. The number of NMR-derived structures deposited in the Protein Data Bank (PDB) is...
nmrlearner
Journal club
0
08-22-2010 03:31 PM
[NMR paper] An automated approach for defining core atoms and domains in an ensemble of NMR-deriv
An automated approach for defining core atoms and domains in an ensemble of NMR-derived protein structures.
Related Articles An automated approach for defining core atoms and domains in an ensemble of NMR-derived protein structures.
Protein Eng. 1997 Jun;10(6):737-41
Authors: Kelley LA, Gardner SP, Sutcliffe MJ
A single NMR-derived protein structure is usually deposited as an ensemble containing many structures, each consistent with the restraint set used. The number of NMR-derived structures deposited in the Protein Data Bank (PDB) is...
nmrlearner
Journal club
0
08-22-2010 03:03 PM
[NMR paper] Internal mobility in the partially folded DNA binding and dimerization domains of GAL
Internal mobility in the partially folded DNA binding and dimerization domains of GAL4: NMR analysis of the N-H spectral density functions.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Internal mobility in the partially folded DNA binding and dimerization domains of GAL4: NMR analysis of the N-H spectral density functions.
Biochemistry. 1996 Feb 27;35(8):2674-86
Authors: Lefevre JF, Dayie KT, Peng JW, Wagner G
The DNA binding domain (residues 1--65) of the yeast transcriptional...
nmrlearner
Journal club
0
08-22-2010 02:27 PM
Solution structure of the RBD1,2 domains from human nucleolin
Solution structure of the RBD1,2 domains from human nucleolin
Content Type Journal Article
DOI 10.1007/s10858-010-9412-1
Authors
Sengodagounder Arumugam, University of Louisville JG Brown Cancer Center 505 South Hancock St. Louisville KY 40202 USA
M. Clarke Miller, University of Louisville JG Brown Cancer Center 505 South Hancock St. Louisville KY 40202 USA
James Maliekal, University of Louisville JG Brown Cancer Center 505 South Hancock St. Louisville KY 40202 USA
nmrlearner
Journal club
0
08-14-2010 04:19 AM
Installation of GROMACS 3.3.1 on Dell Inspiron 6400 with Fedora Core 6, Test 3, Dual Core processor
This is not really a "hard-core NMR topic" but it could be useful for people who try to complement dynamics data from NMR relaxation experiments with MD simulations.
I had really hard time trying to install the newer versions of Gromacs 3.3 and 3.3.1 on my laptop (Dell Inspiron 6400 Dual Core processor) . The laptop used to run Suse 10.1 that was recently replaced with Fedora Core 6 Test 3 (that finally supports Intel integrated mobile 945 video cards). With both OS, Gromacs 3.3.x could be installed, however, its sub-program "genion" failed (the program never ends while consuming 100%...
NMR spectroscopy reveals the solution dimerization interface of p53 core domains boun
Linear Mode
