Related ArticlesDefining the p53 DNA-binding domain/Bcl-x(L)-binding interface using NMR.
FEBS Lett. 2004 Feb 13;559(1-3):171-4
Authors: Petros AM, Gunasekera A, Xu N, Olejniczak ET, Fesik SW
p53 exerts its tumor suppressor activity through both transcription-dependent and transcription-independent processes. Although the transcription-dependent activity of p53 has been extensively studied, the mechanism for transcription-independent p53-mediated tumor suppression is less well known. Recently, it was reported that p53 can directly induce mitochondrial permeabilization and promote apoptosis. This occurs through complexation of the DNA-binding region of p53 with the anti-apoptotic proteins Bcl-x(L) and Bcl-2 (Mihara, M. et al. (2003) Mol. Cell 11, 577-590). Using nuclear magnetic resonance (NMR) spectroscopy we show that the interaction surface on p53 involves the same region that is used by the protein to contact DNA. The p53-binding site on Bcl-x(L) consists of the carboxy-terminus of the first alpha-helix, the loop between alpha3 and alpha4, and the loop between alpha5 and alpha6 of Bcl-x(L). Furthermore, the interaction of p53 with Bcl-x(L) is blocked by the binding of a 25-residue peptide derived from the BH3 region of the pro-apoptotic protein referred to as Bad.
[NMR paper] Selective interface detection: mapping binding site contacts in membrane proteins by
Selective interface detection: mapping binding site contacts in membrane proteins by NMR spectroscopy.
Related Articles Selective interface detection: mapping binding site contacts in membrane proteins by NMR spectroscopy.
J Am Chem Soc. 2005 Apr 27;127(16):5734-5
Authors: Kiihne SR, Creemers AF, de Grip WJ, Bovee-Geurts PH, Lugtenburg J, de Groot HJ
Intermolecular contact surfaces are important regions where specific interactions mediate biological function. We introduce a new magic angle spinning solid state NMR technique, dubbed "selective...
nmrlearner
Journal club
0
11-25-2010 08:21 PM
[NMR paper] Biochemical and NMR mapping of the interface between CREB-binding protein and ligand
Biochemical and NMR mapping of the interface between CREB-binding protein and ligand binding domains of nuclear receptor: beyond the LXXLL motif.
Related Articles Biochemical and NMR mapping of the interface between CREB-binding protein and ligand binding domains of nuclear receptor: beyond the LXXLL motif.
J Biol Chem. 2005 Feb 18;280(7):5682-92
Authors: Klein FA, Atkinson RA, Potier N, Moras D, Cavarelli J
CBP, cAMP-response element-binding protein (CREB)-binding protein, plays an important role as a general cointegrator of various signaling...
nmrlearner
Journal club
0
11-24-2010 10:03 PM
[NMR paper] Ubiquitin binding interface mapping on yeast ubiquitin hydrolase by NMR chemical shif
Ubiquitin binding interface mapping on yeast ubiquitin hydrolase by NMR chemical shift perturbation.
Related Articles Ubiquitin binding interface mapping on yeast ubiquitin hydrolase by NMR chemical shift perturbation.
Biochemistry. 1999 Jul 20;38(29):9242-53
Authors: Rajesh S, Sakamoto T, Iwamoto-Sugai M, Shibata T, Kohno T, Ito Y
The interaction between the 26 kDa yeast ubiquitin hydrolase (YUH1), involved in maintaining the monomeric ubiquitin pool in cells, and the 8.5 kDa yeast ubiquitin protein has been studied by heteronuclear...
nmrlearner
Journal club
0
11-18-2010 08:31 PM
[NMR paper] Characterization of the binding interface between ubiquitin and class I human ubiquit
Characterization of the binding interface between ubiquitin and class I human ubiquitin-conjugating enzyme 2b by multidimensional heteronuclear NMR spectroscopy in solution.
Related Articles Characterization of the binding interface between ubiquitin and class I human ubiquitin-conjugating enzyme 2b by multidimensional heteronuclear NMR spectroscopy in solution.
J Mol Biol. 1999 Jul 2;290(1):213-28
Authors: Miura T, Klaus W, Gsell B, Miyamoto C, Senn H
Ubiquitin-conjugating enzymes (Ubc) are involved in ubiquitination of proteins in the...
nmrlearner
Journal club
0
11-18-2010 08:31 PM
[NMR paper] 1H, 15N, and 13C NMR resonance assignments for the DNA-binding domain of the BPV-1 E2
1H, 15N, and 13C NMR resonance assignments for the DNA-binding domain of the BPV-1 E2 protein.
Related Articles 1H, 15N, and 13C NMR resonance assignments for the DNA-binding domain of the BPV-1 E2 protein.
J Biomol NMR. 1998 May;11(4):457-8
Authors: Veeraraghavan S, Mello CC, Lee KM, Androphy EJ, Baleja JD
nmrlearner
Journal club
0
11-17-2010 11:06 PM
Defining a Stem Length-Dependent Binding Mechanism for the Cocaine-Binding Aptamer. A
Defining a Stem Length-Dependent Binding Mechanism for the Cocaine-Binding Aptamer. A Combined NMR and Calorimetry Study
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi100952k/aop/images/medium/bi-2010-00952k_0010.gif
Biochemistry
DOI: 10.1021/bi100952k
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/HDHRgmphxQs
More...
nmrlearner
Journal club
0
09-08-2010 07:29 AM
[NMR paper] NMR spectroscopic studies of the DNA-binding domain of the monomer-binding nuclear or
NMR spectroscopic studies of the DNA-binding domain of the monomer-binding nuclear orphan receptor, human estrogen related receptor-2. The carboxyl-terminal extension to the zinc-finger region is unstructured in the free form of the protein.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-standard-jbc_full_free.gif Related Articles NMR spectroscopic studies of the DNA-binding domain of the monomer-binding nuclear orphan receptor, human estrogen related receptor-2. The carboxyl-terminal extension to the zinc-finger region...