The immunosuppressant FK506 binds Plasmodium falciparum FK-506 binding protein 35 (PfFKBP35) and shows anti-malarial activity. To understand molecular mechanism of the drug on the parasite, we have done NMR studies. Here, we report the assignment of FK506-binding domain of PfFKBP35.
Salmonella typhimurium OppA is the periplasmic oligopeptide-binding protein. Backbone resonances of OppA(D419N) on its own were assigned for ∼90% of residues. Missing residues are localised around the ligand-binding site, suggesting conformational flexibility in the unliganded state.
We have assigned 1H, 15N and 13C resonances of the RGS domain from the human RGS14 protein, a multi-domain member of the RGS (Regulators of G-protein signalling) family of proteins, important in the down-regulation of specific G-protein signalling pathways.
SUMO (small ubiquitin-like modifier) plays important roles in diverse processes by posttranslationally modifying many proteins. Here we report the resonance assignment of the truncated SUMO from Trypanosoma brucei.
To facilitate NMR spectroscopy studies of interactions with various ligands and potential inhibitors, we report the NMR backbone resonance assignments for the 26 kD human enzyme UCH-L3, a member of the ubiquitin C-hydrolase family of ubiquitin-specific cysteine proteases.
We have determined 13C/15N/1H assignments for the reduced and oxidised forms of Vibrio cholerae DsbA (VcDsbA). These form the basis for ongoing studies aimed at characterising the dynamics observed in the different redox forms of this bacterial oxidoreductase enzyme.
A family of Clostridium perfringens glycoside hydrolases (CpGH84A-E), with a conserved family 84 catalytic module, are thought to target the gastric mucosal layer. Chemical shift assignments have been completed for a putative protein-protein interaction X82 module from CpGH84C.
The family of CRP proteins comprises three members, which are composed of two LIM domains separated by a long linker of more than 50 residues. We determined the structure of the muscle variant, MLP (CRP3), by nuclear magnetic resonance and show that the two LIM domains are independent of each other.
Complete 13C and 15N assignments of the B3 IgG-binding domain of protein G (GB3) in the microcrystalline solid phase, obtained using 2D and 3D MAS NMR, are presented. The chemical shifts are used to predict the protein backbone conformation and compared with solution-state shifts.
The ampG gene codes for a permease required to uptake anhydro-muropeptides into bacterial cytoplasm. Located upstream in the same operon, is another 579-base-pair-long open reading frame encoding a putative lipoprotein YajG, whose nearly complete 1H,13C,15N assignments are reported here.
We report the almost complete assignment of 1H, 13C and 15N nuclei in the 137-residue his-tagged fasciclin domain protein (Fdp) from Rhodobacter sphaeroides. Fdp is homologous to fasciclin I domains, including Drosophila FAS1 and M. tuberculosis MPB70 and plays a role in cell adhesion.
Calcium-binding protein 1 (CaBP1) regulates inositol 1,4,5-trisphosphate receptors (InsP3Rs) and a variety of voltage-gated Ca2+ channels in the brain. We report complete NMR chemical shift assignments of Ca2+-free CaBP1 (residues 1–167, BMRB no. 15197).
Isotopically labeled, 15N and 15N/13C forms of recombinant methionine-r-sulfoxide reductase 1 (MsrB1, SelR) from Mus musculus were produced, in which catalytic selenocysteine was replaced with cysteine. We report here the 1H, 15N and 13C NMR assignment of the reduced form of this mammalian protein.
Rheb (Ras homologue enriched in brain) is a small GTPase that plays an important role in tuberous sclerosis. Here we present the backbone assignments of rRheb in its GDP-bound state. These assignments now provide a basis for the analysis of the interaction of rRheb with putative factors in order to elucidate the function of this GTPase and its role in the MAP kinase pathway of neuronal cells and in...
Here we report the NMR resonance assignments for the reduced form of human IgG1 CH3 domain, a 26 kDa dimer in solution (residues 341–447). The assignments have been deposited in the BioMagResBank with a BMRB accession number of 15204.
We report 1H, 15N and 13C resonance assignments for the small G protein RalB in its active conformation. Backbone amide dynamics parameters for a majority of residues have also been obtained. The BMRB accession code is 15320.
We report the nearly complete 1H, 13C and 15N resonance assignments of the oxidized form (Cys67–Cys70) of the N-terminal domain of PilB from Neisseria meningitidis. Secondary structure determination using CSI method and TALOS leads mainly to the prediction of 7 α-helical and 5 β-sheet parts.
Nix protein is a BH3-only pro-apoptotic mitochondrial protein. Here we reported the 1H, 13C and 15N resonance assignments of zebrafish Nix protein for further understanding the structure and function relationship.
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