NMR paper Prion protein interaction with the C-terminal SH3 domain of Grb2 studied using NMR an

		BioNMR > Educational resources > Journal club
[NMR paper] Prion protein interaction with the C-terminal SH3 domain of Grb2 studied using NMR an

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

11-24-2010, 10:01 PM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,777

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

Prion protein interaction with the C-terminal SH3 domain of Grb2 studied using NMR an

Prion protein interaction with the C-terminal SH3 domain of Grb2 studied using NMR and optical spectroscopy.

Related Articles Prion protein interaction with the C-terminal SH3 domain of Grb2 studied using NMR and optical spectroscopy.

Biochemistry. 2004 Aug 17;43(32):10393-9

Authors: Lysek DA, Wüthrich K

Transmissible spongiform encephalopathies have been observed exclusively in organisms expressing the host-encoded prion protein (PrP). The function of the cellular isoform of PrP found in healthy organisms has so far not been identified, although there are indications of a role in signal transduction in neurons. To gain further insight into the functional properties of cellular PrP, this paper investigated the binding of the C-terminal SH3 domain of the murine growth factor receptor-bound protein 2 (Grb2) to the murine PrP, using NMR, fluorescence, and circular dichroism spectroscopy. The SH3-binding site in murine PrP was thus found to be in the highly conserved region of residues 100-109, which contains prolines in positions 101 and 104. The protein-protein interaction, with a K(D) value of 5.5 microM, is abolished when either of these two prolines is replaced by leucine. In humans, two corresponding Pro --> Leu exchanges are found in patients who present with the Gerstmann-Sträussler-Scheinker syndrome. The results of the present study thus indicate a possible mechanism by which amino acid exchanges could influence a specific protein-protein interaction in a complex signal transduction cascade, which might be of functional significance in health and disease.

PMID: 15301538 [PubMed - indexed for MEDLINE]

Source: PubMed

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
Extensive de novo solid-state NMR assignments of the 33 kDa C-terminal domain of the Ure2 prion Extensive de novo solid-state NMR assignments of the 33 kDa C-terminal domain of the Ure2 prion Abstract We present the de novo resonance assignments for the crystalline 33 kDa C-terminal domain of the Ure2 prion using an optimized set of five 3D solid-state NMR spectra. We obtained, using a single uniformly 13C, 15N labeled protein sample, sequential chemical-shift information for 74% of the N, CÎ±, CÎ² triples, and for 80% of further side-chain resonances for these spin systems. We describe the procedures and protocols devised, and discuss possibilities and limitations of the...	nmrlearner	Journal club	0	08-04-2011 01:14 AM
Extensive de novo solid-state NMR assignments of the 33kDa C-terminal domain of the Ure2 prion. Extensive de novo solid-state NMR assignments of the 33kDa C-terminal domain of the Ure2 prion. Extensive de novo solid-state NMR assignments of the 33kDa C-terminal domain of the Ure2 prion. J Biomol NMR. 2011 Jul 31; Authors: Habenstein B, Wasmer C, Bousset L, Sourigues Y, Schütz A, Loquet A, Meier BH, Melki R, Böckmann A We present the de novo resonance assignments for the crystalline 33kDa C-terminal domain of the Ure2 prion using an optimized set of five 3D solid-state NMR spectra. We obtained, using a single uniformly (13)C, (15)N labeled...	nmrlearner	Journal club	0	08-02-2011 11:40 AM
[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 structure of the N-terminal domain of SUMO ligase PIAS1 and its interaction with NMR structure of the N-terminal domain of SUMO ligase PIAS1 and its interaction with tumor suppressor p53 and A/T-rich DNA oligomers. Related Articles NMR structure of the N-terminal domain of SUMO ligase PIAS1 and its interaction with tumor suppressor p53 and A/T-rich DNA oligomers. J Biol Chem. 2004 Jul 23;279(30):31455-61 Authors: Okubo S, Hara F, Tsuchida Y, Shimotakahara S, Suzuki S, Hatanaka H, Yokoyama S, Tanaka H, Yasuda H, Shindo H A member of the PIAS (protein inhibitor of activated STAT) family of proteins, PIAS1, have been reported...	nmrlearner	Journal club	0	11-24-2010 09:51 PM
NMR solution structure of the N-terminal domain of hERG and its interaction with the NMR solution structure of the N-terminal domain of hERG and its interaction with the S4-S5 linker. NMR solution structure of the N-terminal domain of hERG and its interaction with the S4-S5 linker. Biochem Biophys Res Commun. 2010 Nov 2; Authors: Li Q, Gayen S, Chen AS, Huang Q, Raida M, Kang C The human Ether-à-go-go Related Gene (hERG) potassium channel mediates the rapid delayed rectifier current (IKr) in the cardiac action potential. Mutations in the 135 amino acid residue N-terminal domain (NTD) cause channel dysfunction or...	nmrlearner	Journal club	0	11-09-2010 11:29 AM
[NMR paper] Structure of the A-domain of HMG1 and its interaction with DNA as studied by heteronu Structure of the A-domain of HMG1 and its interaction with DNA as studied by heteronuclear three- and four-dimensional NMR spectroscopy. Related Articles Structure of the A-domain of HMG1 and its interaction with DNA as studied by heteronuclear three- and four-dimensional NMR spectroscopy. Biochemistry. 1995 Dec 26;34(51):16596-607 Authors: Hardman CH, Broadhurst RW, Raine AR, Grasser KD, Thomas JO, Laue ED HMG1 has two homologous, folded DNA-binding domains ("HMG boxes"), A and B, linked by a short basic region to an acidic C-terminal domain....	nmrlearner	Journal club	0	08-22-2010 03:50 AM
[NMR paper] NMR structure of the N-terminal SH3 domain of GRB2 and its complex with a proline-ric NMR structure of the N-terminal SH3 domain of GRB2 and its complex with a proline-rich peptide from Sos. Related Articles NMR structure of the N-terminal SH3 domain of GRB2 and its complex with a proline-rich peptide from Sos. Nat Struct Biol. 1994 Dec;1(12):898-907 Authors: Goudreau N, Cornille F, Duchesne M, Parker F, TocquÃ© B, Garbay C, Roques BP GRB2 is a small adaptor protein of 217 amino acids comprising one SH2 domain surrounded by two SH3 domains. GRB2 couples receptor tyrosine kinase activation to Ras signalling by interacting,...	nmrlearner	Journal club	0	08-22-2010 03:29 AM
[NMR paper] 1H-NMR investigation of the interaction of the amino terminal domain of the LexA repr 1H-NMR investigation of the interaction of the amino terminal domain of the LexA repressor with a synthetic half-operator. Related Articles 1H-NMR investigation of the interaction of the amino terminal domain of the LexA repressor with a synthetic half-operator. J Biomol Struct Dyn. 1991 Dec;9(3):447-61 Authors: Ottleben G, Messori L, RÃ¼terjans H, Kaptein R, Granger-Schnarr M, Schnarr M A synthetic half-operator DNA-duplex, d(GCTACTGTATGT), containing a portion of the proposed recognition sequence (CTGT) of several "SOS" genes, has been...	nmrlearner	Journal club	0	08-21-2010 11:12 PM

« 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