NMR paper Interaction of the bHLH-zip domain of c-Myc with H1-type peptides. Characterization o

		BioNMR > Educational resources > Journal club
[NMR paper] Interaction of the bHLH-zip domain of c-Myc with H1-type peptides. Characterization o

Webservers

NMR processing:

MDD

NMR assignment:

Backbone:

Side-chains:

NOEs:

Structure from NMR restraints:

Ab initio:

Fragment-based:

Rosetta-NMR (Robetta)

Template-based:

GeNMR

I-TASSER

Refinement:

Amber

Structure from chemical shifts:

Fragment-based:

Homology-based:

Torsion angles from chemical shifts:

Preditor

TALOS

Promega- Proline

Secondary structure from chemical shifts:

CSI (via RCI server)

TALOS

MICS caps, β-turns

d2D

PECAN

Flexibility from chemical shifts:

RCI

Interactions from chemical shifts:

HADDOCK

Chemical shifts re-referencing:

NMR model quality:

NOEs, other restraints:

Chemical shifts:

RDCs:

Pseudocontact shifts:

Protein geomtery:

SAVES2 or SAVES4

Quality Control Check

NMR spectrum prediction:

FANDAS

MestReS

V-NMR

Flexibility from structure:

Backbone S2

Methyl S2

B-factor

Molecular dynamics:

Gromacs

Amber

Antechamber

Chemical shifts prediction:

From structure:

Shiftx2

Sparta+

Camshift

CH3shift- Methyl

ArShift- Aromatic

ShiftS

Proshift

PPM

CheShift-2- Cα

From sequence:

Shifty

Camcoil

Poulsen_rc_CS

Disordered proteins:

MAXOCC

Format conversion & validation:

CCPN

From NMR-STAR 3.1

Validate NMR-STAR 3.1

NMR sample preparation:

Protein disorder:

DisMeta

Protein solubility:

Isotope labeling:

Solid-state NMR:

Thread Tools

Search this Thread

Rate Thread

Display Modes

08-22-2010, 03:33 AM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,733

Points: 193,617, Level: 100

Level up: 0%, 0 Points needed

Activity: 50.7%

Last Achievements

Award-Showcase

NMR Credits: 0

NMR Points: 193,617

Downloads: 0

Uploads: 0

Interaction of the bHLH-zip domain of c-Myc with H1-type peptides. Characterization o

Interaction of the bHLH-zip domain of c-Myc with H1-type peptides. Characterization of helicity in the H1 peptides by NMR.

Related Articles Interaction of the bHLH-zip domain of c-Myc with H1-type peptides. Characterization of helicity in the H1 peptides by NMR.

J Biol Chem. 1994 Jan 21;269(3):1785-93

Authors: Draeger LJ, Mullen GP

The carboxyl-terminal 92 residues of c-Myc-92 display site-specific DNA binding specificity for the consensus sequence 5'-CACCACGTGGTG-3' (Blackwell, T. K., Kretzner, L., Blackwood, E. M., Eisenman, R. N., and Weintraub, H. (1990) Science 250, 1149-1151). Size exclusion high pressure liquid chromatography analysis of the purified fusion protein, glutathione S-transferase-c-Myc-92, indicates that c-Myc-92 is tetrameric with a dissociation constant of < 60 nM. Helix-1 (H1) and leucine zipper peptides from the basic-helix-loop-helix-zipper domain of c-Myc and Max were assayed as potential inhibitors of c-Myc-92 DNA binding. H1 peptides with substitutions that confer greater helicity are found to inhibit c-Myc-92 DNA binding. The mechanism of inhibition involves the cooperative binding of H1 peptides with tetrameric c-Myc-92 as determined by a spectrophotometric assay employing 2,4-dinitrophenyl-H1-F8A. NMR structural characterization reveals a correlation between helicity and inhibition. In a partially hydrophobic environment, H1-Mx (from Max) is a random coil, while H1-WT, H1-F8A, and H1-F8A,S6A (from c-Myc) display differing degrees of helicity. Structure determination on the basis of nuclear Overhauser effect data indicates that the H1-F8A helix is significantly more ordered than H1-WT. Analysis on the basis of the Max x-ray structure (FerrÃ©-D'AmarÃ©, R., Prendergast, G. C., Ziff, E. B., and Burley, S. K. (1993) Nature 363, 38-45) suggests that H1 peptide binding to c-Myc-92 may occur through an alteration in the packing of helix-1 in c-Myc-92 or through an interaction with an exposed hydrophobic cluster of residues at each H1-H2 interface. This binding site for H1 peptides may be of significance in the interaction of c-Myc with proteins involved in transcriptional regulation.

PMID: 8294427 [PubMed - indexed for MEDLINE]

Source: PubMed

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
[NMR paper] Interaction between the type-3 copper protein tyrosinase and the substrate analogue p Interaction between the type-3 copper protein tyrosinase and the substrate analogue p-nitrophenol studied by NMR. Related Articles Interaction between the type-3 copper protein tyrosinase and the substrate analogue p-nitrophenol studied by NMR. J Am Chem Soc. 2005 Jan 19;127(2):567-75 Authors: Tepper AW, Bubacco L, Canters GW The interaction of the monooxygenating type-3 copper enzyme Tyrosinase (Ty) from Streptomyces antibioticus with its inhibitor p-nitrophenol (pnp) was studied by paramagnetic NMR methods. The pnp binds to oxidized Ty...	nmrlearner	Journal club	0	11-24-2010 11:14 PM
[NMR paper] NMR characterization of the interaction between the C-terminal domain of interferon-g NMR characterization of the interaction between the C-terminal domain of interferon-gamma and heparin-derived oligosaccharides. Related Articles NMR characterization of the interaction between the C-terminal domain of interferon-gamma and heparin-derived oligosaccharides. Biochem J. 2004 Nov 15;384(Pt 1):93-9 Authors: Vanhaverbeke C, Simorre JP, Sadir R, Gans P, Lortat-Jacob H Interferons are cytokines that play a complex role in the resistance of mammalian hosts to pathogens. IFNgamma (interferon-gamma) is secreted by activated T-cells and...	nmrlearner	Journal club	0	11-24-2010 10:03 PM
[NMR paper] NMR and MD studies on the interaction between ligand peptides and alpha-bungarotoxin. NMR and MD studies on the interaction between ligand peptides and alpha-bungarotoxin. Related Articles NMR and MD studies on the interaction between ligand peptides and alpha-bungarotoxin. J Mol Biol. 2004 Jun 18;339(5):1169-77 Authors: Bernini A, Ciutti A, Spiga O, Scarselli M, Klein S, Vannetti S, Bracci L, Lozzi L, Lelli B, Falciani C, Neri P, Niccolai N The interaction between alpha-bungarotoxin and linear synthetic peptides, mimotope of the nicotinic acetylcholine receptor binding site, has been characterised extensively by several...	nmrlearner	Journal club	0	11-24-2010 09:51 PM
[NMR paper] A strategy for the NMR characterization of type II copper(II) proteins: the case of t A strategy for the NMR characterization of type II copper(II) proteins: the case of the copper trafficking protein CopC from Pseudomonas Syringae. Related Articles A strategy for the NMR characterization of type II copper(II) proteins: the case of the copper trafficking protein CopC from Pseudomonas Syringae. J Am Chem Soc. 2003 Jun 18;125(24):7200-8 Authors: Arnesano F, Banci L, Bertini I, Felli IC, Luchinat C, Thompsett AR CopC from Pseudomonas syringae was found to be a protein capable of binding both Cu(I) and Cu(II) at two different...	nmrlearner	Journal club	0	11-24-2010 09:01 PM
[NMR paper] 1H NMR study on the binding of Pin1 Trp-Trp domain with phosphothreonine peptides. 1H NMR study on the binding of Pin1 Trp-Trp domain with phosphothreonine peptides. Related Articles 1H NMR study on the binding of Pin1 Trp-Trp domain with phosphothreonine peptides. J Biol Chem. 2001 Jul 6;276(27):25150-6 Authors: Wintjens R, Wieruszeski JM, Drobecq H, Rousselot-Pailley P, Buée L, Lippens G, Landrieu I The recent crystal structure of Pin1 protein bound to a doubly phosphorylated peptide from the C-terminal domain of RNA polymerase II revealed that binding interactions between Pin1 and its substrate take place through its...	nmrlearner	Journal club	0	11-19-2010 08:32 PM
[NMR paper] Interaction of a type II myosin with biological membranes studied by 2H solid state N Interaction of a type II myosin with biological membranes studied by 2H solid state NMR. Related Articles Interaction of a type II myosin with biological membranes studied by 2H solid state NMR. Biochemistry. 1998 Apr 21;37(16):5582-8 Authors: Arêas JA, Gröbner G, Glaubitz C, Watts A Deuterium nuclear magnetic resonance spectroscopy (2H NMR) has been employed to investigate the interaction of lung type II myosin protein with neutral bilayers containing dimyristoylphosphatidylcholine (DMPC) as the only constituent and mixed bilayers containing...	nmrlearner	Journal club	0	11-17-2010 11:06 PM
[NMR paper] CD and NMR structural characterization of ceratotoxins, natural peptides with antimic CD and NMR structural characterization of ceratotoxins, natural peptides with antimicrobial activity. Related Articles CD and NMR structural characterization of ceratotoxins, natural peptides with antimicrobial activity. Biopolymers. 1996 Nov;39(5):653-64 Authors: Ragona L, Molinari H, Zetta L, Longhi R, Marchini D, Dallai R, Bernini LF, Lozzi L, Scarselli M, Niccolai N Antibacterial properties of the secretion from the female reproductive accessory glands of medfly Ceratitis capitata are mostly ascribed to the presence of two peptides,...	nmrlearner	Journal club	0	08-22-2010 02:20 PM
[NMR paper] Interaction of the bHLH-zip domain of c-Myc with H1-type peptides. Characterization o Interaction of the bHLH-zip domain of c-Myc with H1-type peptides. Characterization of helicity in the H1 peptides by NMR. Related Articles Interaction of the bHLH-zip domain of c-Myc with H1-type peptides. Characterization of helicity in the H1 peptides by NMR. J Biol Chem. 1994 Jan 21;269(3):1785-93 Authors: Draeger LJ, Mullen GP The carboxyl-terminal 92 residues of c-Myc-92 display site-specific DNA binding specificity for the consensus sequence 5'-CACCACGTGGTG-3' (Blackwell, T. K., Kretzner, L., Blackwood, E. M., Eisenman, R. N., and...	nmrlearner	Journal club	0	08-22-2010 03:33 AM

« Previous Thread | Next Thread »

Posting Rules
You may not post new threads You may not post replies You may not post attachments You may not edit your posts BB code is On Smilies are On [IMG] code is On HTML code is On Trackbacks are Off Pingbacks are Off Refbacks are Off