[NMR paper] Structural insight into the interaction of O-acetylserine sulfhydrylase with competitive, peptidic inhibitors by saturation transfer difference-NMR.
Related ArticlesStructural insight into the interaction of O-acetylserine sulfhydrylase with competitive, peptidic inhibitors by saturation transfer difference-NMR.
FEBS Lett. 2016 Apr;590(7):943-53
Authors: Benoni R, Pertinhez TA, Spyrakis F, Davalli S, Pellegrino S, Paredi G, Pezzotti A, Bettati S, Campanini B, Mozzarelli A
Abstract
O-acetylserine sulfhydrylase (OASS), the enzyme catalysing the last step of cysteine biosynthesis in bacteria, is involved in antibiotic resistance and biofilm formation. Since mammals lack OASS, it is a potential target for antimicrobials. However, a limited number of inhibitors has been developed and crystallized in complex with OASS. STD-NMR was applied to study the interaction of the inhibitory pentapeptide MNYDI with the CysK and CysM OASS isozymes from Salmonella Typhimurium. Results are in excellent agreement with docking and SAR studies and confirm the important role played by the C-terminal Ile5 and the arylic moiety at P3 in dictating affinity.
[NMR paper] Molecular Level Insights on Collagen-Polyphenols Interaction using Spin-Relaxation and Saturation Transfer Difference NMR.
Molecular Level Insights on Collagen-Polyphenols Interaction using Spin-Relaxation and Saturation Transfer Difference NMR.
Related Articles Molecular Level Insights on Collagen-Polyphenols Interaction using Spin-Relaxation and Saturation Transfer Difference NMR.
J Phys Chem B. 2015 Oct 8;
Authors: Reddy RR, Phani Kumar BV, Shanmugam G, Madhan B, Mandal AB
Abstract
Interaction of small molecules with collagen has far reaching consequences in biological and industrial processes. The interaction between collagen and selected...
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[NMR paper] Structural Analysis of CXCR4 - Antagonist Interactions Using Saturation-Transfer Double-Difference NMR.
Structural Analysis of CXCR4 - Antagonist Interactions Using Saturation-Transfer Double-Difference NMR.
Related Articles Structural Analysis of CXCR4 - Antagonist Interactions Using Saturation-Transfer Double-Difference NMR.
Biochem Biophys Res Commun. 2015 Aug 21;
Authors: Cox BD, Mehta AK, DiRaddo JO, Liotta DC, Wilson LJ, Snyder JP
Abstract
CXCR4 is a GPCR involved in leukocyte trafficking. Small molecule antagonists of the receptor may treat inflammatory disease, cancer and HIV. Here we probe the binding of a...
[NMR paper] Characterization of heparin-protein interaction by saturation transfer difference (STD) NMR.
Characterization of heparin-protein interaction by saturation transfer difference (STD) NMR.
Related Articles Characterization of heparin-protein interaction by saturation transfer difference (STD) NMR.
Anal Bioanal Chem. 2014 Mar 25;
Authors: Yu F, Roy S, Arevalo E, Schaeck J, Wang J, Holte K, Duffner J, Gunay NS, Capila I, Kaundinya GV
Abstract
The binding affinity and specificity of heparin to proteins is widely recognized to be sulfation-pattern dependent. However, for the majority of heparin-binding proteins (HBPs), it still remains...
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03-26-2014 12:44 PM
[NMR paper] Role of 2-Hydroxyethyl Methacrylate in the Interaction of Dental Monomers with Collagen Studied by Saturation Transfer Difference NMR.
Role of 2-Hydroxyethyl Methacrylate in the Interaction of Dental Monomers with Collagen Studied by Saturation Transfer Difference NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Role of 2-Hydroxyethyl Methacrylate in the Interaction of Dental Monomers with Collagen Studied by Saturation Transfer Difference NMR.
J Dent. 2014 Jan 16;
Authors: Hiraishi N, Tochio N, Kigawa T, Otsuki M, Tagam J
Abstract
Objections: Functional adhesive monomers...
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01-21-2014 11:10 PM
The interaction of La(3+) complexes of DOTA/DTPA glycoconjugates with the RCA(120) lectin: a saturation transfer difference NMR spectroscopic study.
The interaction of La(3+) complexes of DOTA/DTPA glycoconjugates with the RCA(120) lectin: a saturation transfer difference NMR spectroscopic study.
The interaction of La(3+) complexes of DOTA/DTPA glycoconjugates with the RCA(120) lectin: a saturation transfer difference NMR spectroscopic study.
J Biol Inorg Chem. 2011 Apr 3;
Authors: Teixeira JM, Dias DM, Cañada FJ, Martins JA, André JP, Jiménez-Barbero J, Geraldes CF
The study of ligand-receptor interactions using high-resolution NMR techniques, namely the saturation transfer difference (STD),...
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04-05-2011 10:22 PM
[NMR paper] Probing specific lipid-protein interaction by saturation transfer difference NMR spectroscopy.
Probing specific lipid-protein interaction by saturation transfer difference NMR spectroscopy.
Related Articles Probing specific lipid-protein interaction by saturation transfer difference NMR spectroscopy.
J Am Chem Soc. 2005 Sep 28;127(38):13110-1
Authors: Soubias O, Gawrisch K
We studied the interaction of mono- and polyunsaturated phosphatidylcholines with rhodopsin by 1H NMR saturation transfer difference spectroscopy with magic angle spinning (STD-MAS NMR). The results indicate a strong preference for interaction of rhodopsin with the...
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[NMR paper] pH dependence of the absorbance and 31P NMR spectra of O-acetylserine sulfhydrylase i
pH dependence of the absorbance and 31P NMR spectra of O-acetylserine sulfhydrylase in the absence and presence of O-acetyl-L-serine.
Related Articles pH dependence of the absorbance and 31P NMR spectra of O-acetylserine sulfhydrylase in the absence and presence of O-acetyl-L-serine.
Biochemistry. 1992 Mar 3;31(8):2298-303
Authors: Cook PF, Hara S, Nalabolu S, Schnackerz KD
O-Acetylserine sulfhydrylase (OASS) is a pyridoxal 5'-phosphate (PLP)-dependent enzyme which catalyzes the final step in the biosynthesis of L-cysteine in Salmonella, viz.,...
Structural insight into the interaction of O-acetylserine sulfhydrylase with competitive, peptidic inhibitors by saturation transfer difference-NMR.
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