NMR paper NMR study of the interaction between the B domain of staphylococcal protein A and the

		BioNMR > Educational resources > Journal club
[NMR paper] NMR study of the interaction between the B domain of staphylococcal protein A and the

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

11-17-2010, 11:06 PM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,700

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

NMR study of the interaction between the B domain of staphylococcal protein A and the

NMR study of the interaction between the B domain of staphylococcal protein A and the Fc portion of immunoglobulin G.

Related Articles NMR study of the interaction between the B domain of staphylococcal protein A and the Fc portion of immunoglobulin G.

Biochemistry. 1998 Jan 6;37(1):129-36

Authors: Gouda H, Shiraishi M, Takahashi H, Kato K, Torigoe H, Arata Y, Shimada I

The solution structure of the B domain of staphylococcal protein A (FB) complexed with the Fc fragment of immunoglobulin G (IgG) is reported. A previous NMR analysis has shown that in solution FB is composed of a bundle of three alpha-helices, helix I, helix II, and helix III [Gouda, H., Torigoe, H., Saito, A., Sato, M., Arata, Y., and Shimada, I. (1992) Biochemistry 31, 9665-9672]. In contrast, the crystal structure of FB in the FB-Fc complex lacks helix III. Uniformly 15N- and 15N/13C-labeled FB were prepared, and the backbone 13C resonances were assigned. The spectral data obtained in the present study indicated that in solution all three helices including helix III are preserved in the FB-Fc complex. The mode of interaction of FB with the Fc fragment was discussed on the basis of the combined data of hydrogen-deuterium exchange experiments and 1H-15N correlation spectroscopy. It was concluded that a contiguous surface shaped by F14, Y15, E16, L18, and H19 in helix I, and N29, Q33, L35, and K36 in helix II is responsible for the binding.

PMID: 9425032 [PubMed - indexed for MEDLINE]

Source: PubMed

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
[NMR paper] A NMR study of the interaction of a three-domain construct of ATP7A with copper(I) and copper(I)-HAH1: the interplay of domains. A NMR study of the interaction of a three-domain construct of ATP7A with copper(I) and copper(I)-HAH1: the interplay of domains. Related Articles A NMR study of the interaction of a three-domain construct of ATP7A with copper(I) and copper(I)-HAH1: the interplay of domains. J Biol Chem. 2005 Nov 18;280(46):38259-63 Authors: Banci L, Bertini I, Cantini F, Chasapis CT, Hadjiliadis N, Rosato A ATP7A is a P-type ATPase involved in copper(I) homeostasis in humans. It possesses a long N-terminal tail protruding into the cytosol and containing six...	nmrlearner	Journal club	0	12-01-2010 06:56 PM
[NMR paper] 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,...	nmrlearner	Journal club	0	11-24-2010 10:01 PM
[NMR paper] NMR assignment of human ASC2, a self contained protein interaction domain involved in NMR assignment of human ASC2, a self contained protein interaction domain involved in apoptosis and inflammation. Related Articles NMR assignment of human ASC2, a self contained protein interaction domain involved in apoptosis and inflammation. J Biomol NMR. 2002 Jun;23(2):151-2 Authors: Espejo F, Green M, Preece NE, Assa-Munt N	nmrlearner	Journal club	0	11-24-2010 08:49 PM
[NMR paper] NMR study on the interaction between MHC class I protein and its antigen peptide. NMR study on the interaction between MHC class I protein and its antigen peptide. Related Articles NMR study on the interaction between MHC class I protein and its antigen peptide. Biochem Biophys Res Commun. 2000 Nov 30;278(3):609-13 Authors: Nakagawa M, Chiba-Kamoshida K, Udaka K, Nakanishi H A major histcompatibility complex (MHC) class I protein H-2K(b) was expressed in a large scale as a fusion protein with thioredoxin and hexahistidine at the N-terminus to analyze the interaction with the antigen peptide SIYRYYGL. NMR spectra of the...	nmrlearner	Journal club	0	11-19-2010 08:29 PM
[NMR paper] NMR diffusion and relaxation study of drug-protein interaction. NMR diffusion and relaxation study of drug-protein interaction. Related Articles NMR diffusion and relaxation study of drug-protein interaction. Spectrochim Acta A Mol Biomol Spectrosc. 1999 Aug;55A(9):1897-901 Authors: Luo RS, Liu ML, Mao XA In this work, NMR diffusion and relaxation measurements are applied to the study of the interaction between the anti-inflammatory drug salicylate and the human serum albumin (HSA) in solutions. The self-diffusion coefficients and the spin-lattice relaxation rates of salicylate are measured as a function...	nmrlearner	Journal club	0	11-18-2010 08:31 PM
[NMR paper] High-resolution solution NMR structure of the Z domain of staphylococcal protein A. High-resolution solution NMR structure of the Z domain of staphylococcal protein A. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles High-resolution solution NMR structure of the Z domain of staphylococcal protein A. J Mol Biol. 1997 Oct 3;272(4):573-90 Authors: Tashiro M, Tejero R, Zimmerman DE, Celda B, Nilsson B, Montelione GT Staphylococcal protein A (SpA) is a cell-wall-bound pathogenicity factor from the bacterium Staphylococcus aureus. Because of their small size...	nmrlearner	Journal club	0	08-22-2010 05:08 PM
[NMR paper] NMR structure of a protein kinase C-gamma phorbol-binding domain and study of protein NMR structure of a protein kinase C-gamma phorbol-binding domain and study of protein-lipid micelle interactions. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles NMR structure of a protein kinase C-gamma phorbol-binding domain and study of protein-lipid micelle interactions. Biochemistry. 1997 Sep 2;36(35):10709-17 Authors: Xu RX, Pawelczyk T, Xia TH, Brown SC Classical protein kinase C (PKC) family members are activated by the binding of various ligands to one of several cysteine-rich...	nmrlearner	Journal club	0	08-22-2010 05:08 PM
[NMR paper] Accretion of structure in staphylococcal nuclease: an 15N NMR relaxation study. Accretion of structure in staphylococcal nuclease: an 15N NMR relaxation study. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Accretion of structure in staphylococcal nuclease: an 15N NMR relaxation study. J Mol Biol. 1996 Jul 26;260(4):570-87 Authors: Alexandrescu AT, Jahnke W, Wiltscheck R, Blommers MJ 15N main-chain dynamics are compared in four forms of staphylococcal nuclease with different stabilities to unfolding: (1) SN-T, the ternary complex of the protein,...	nmrlearner	Journal club	0	08-22-2010 02:20 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