Related ArticlesStudies on the three-dimensional behaviour of the selectin ligands Lewis(a) and sulphated Lewis(a) using NMR spectroscopy and molecular dynamics simulations.
Glycobiology. 1994 Feb;4(1):49-57
Authors: Kogelberg H, Rutherford TJ
Sulphated blood group Lewis(a)/Lewis(x) (Le(a)/Le(x)) type sequences, with sulphate at the 3-position of galactose, have emerged as potent ligands for the endothelial adhesion molecule E-selectin and the leukocyte adhesion molecule L-selectin. As a first step in elucidating the molecular basis of the strong interactions with the selectins, we have performed conformational studies of the sulphated Le(a) in comparison with the non-sulphated analogue which is less strongly bound by E-selectin and not at all by L-selectin. Experimental NMR parameters [nuclear Overhauser effects (NOE) and interglycosidic 3JC,H] and theoretical values back-calculated from the minimum energy structures are in excellent agreement for both molecules. Molecular dynamics calculations for SuLe(a) depict only minor torsional fluctuations around the glycosidic linkages over the time course of the 500 ps simulations, leading to the conclusion that the conformation of SuLe(a) approximates to a single-rigid structure, as does the previously investigated Le(a) molecule. Comparison of experimentally and theoretically obtained parameters for SuLe(a) with those for the non-sulphated Le(a) molecule indicate that no detectable changes occur in the three-dimensional structure of the trisaccharide upon sulphation. Thus, the enhanced selectin binding to the sulphated Le(a) is most likely due to favourable electrostatic interactions between the charged sulphate group and corresponding charged groups on the selectin protein.
[NMR900 blog] Recognition: Lewis Kay
Recognition: Lewis Kay
Special issue of the Journal of Biomolecular NMR on the occasion of Prof. Lewis E. Kay’s 50th birthday, volume 51, numbers 1-2, September 2011.
Kevin H. Gardner, Anthony Mittermaier and Frans A.A. Mulder, "A tribute to Lewis E. Kay on his 50th birthday" Journal of Biomolecular NMR 51 (2011) 3-4. (Editorial) http://dx.doi.org/10.1007/s10858-011-9561-x
A fitting collection of 18 research publications by colleagues, friends and former students of Lewis Kay to celebrate his many pioneering contributions to the field of biomolecular NMR spectroscopy....
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11-18-2011 04:35 AM
A tribute to Lewis E Kay on his 50th birthday
A tribute to Lewis E Kay on his 50th birthday
A tribute to Lewis E Kay on his 50th birthday
Content Type Journal Article
Category Editorial
Pages 3-4
DOI 10.1007/s10858-011-9561-x
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09-30-2011 08:01 PM
[NMR paper] NMR studies for identifying phosphopeptide ligands of the HIV-1 protein Vpu binding to the F-box protein beta-TrCP.
NMR studies for identifying phosphopeptide ligands of the HIV-1 protein Vpu binding to the F-box protein beta-TrCP.
Related Articles NMR studies for identifying phosphopeptide ligands of the HIV-1 protein Vpu binding to the F-box protein beta-TrCP.
Peptides. 2006 Jan;27(1):194-210
Authors: Evrard-Todeschi N, Gharbi-Benarous J, Bertho G, Coadou G, Megy S, Benarous R, Girault JP
The human immunodeficiency virus type 1 (HIV-1) Vpu enhances viral particle release and, its interaction with the ubiquitin ligase SCF-beta-TrCP triggers the HIV-1...
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12-01-2010 06:56 PM
[NMR paper] Epitope mapping of sialyl Lewis(x) bound to E-selectin using saturation transfer diff
Epitope mapping of sialyl Lewis(x) bound to E-selectin using saturation transfer difference NMR experiments.
Related Articles Epitope mapping of sialyl Lewis(x) bound to E-selectin using saturation transfer difference NMR experiments.
Glycobiology. 2003 Jun;13(6):435-43
Authors: Rinnbauer M, Ernst B, Wagner B, Magnani J, Benie AJ, Peters T
A complex between sialyl Lewisx (alpha-D-Neu5Ac-- beta-D-Gal---beta-D-GlcNAc-O-8 COOMe) and E-selectin was studied using saturation transfer difference (STD) nuclear magnetic resonance (NMR) experiments....
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11-24-2010 09:01 PM
Solution- and solid-state NMR studies of GPCRs and their ligands (Review).
Solution- and solid-state NMR studies of GPCRs and their ligands (Review).
Related Articles Solution- and solid-state NMR studies of GPCRs and their ligands (Review).
Biochim Biophys Acta. 2010 Oct 14;
Authors: Tapaneeyakorn S, Goddard AD, Oates J, Willis CL, Watts A
G protein-coupled receptors (GPCRs) represent one of the major targets of new drugs on the market given their roles as key membrane receptors in many cellular signalling pathways. Structure-based drug design has potential to be the most reliable method for novel drug discovery....
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10-19-2010 04:51 PM
[NMR paper] Studies on the three-dimensional behaviour of the selectin ligands Lewis(a) and sulph
Studies on the three-dimensional behaviour of the selectin ligands Lewis(a) and sulphated Lewis(a) using NMR spectroscopy and molecular dynamics simulations.
Related Articles Studies on the three-dimensional behaviour of the selectin ligands Lewis(a) and sulphated Lewis(a) using NMR spectroscopy and molecular dynamics simulations.
Glycobiology. 1994 Feb;4(1):49-57
Authors: Kogelberg H, Rutherford TJ
Sulphated blood group Lewis(a)/Lewis(x) (Le(a)/Le(x)) type sequences, with sulphate at the 3-position of galactose, have emerged as potent ligands...
nmrlearner
Journal club
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08-22-2010 03:33 AM
[NMR paper] 15N and 13C NMR studies of ligands bound to the 280,000-dalton protein porphobilinoge
15N and 13C NMR studies of ligands bound to the 280,000-dalton protein porphobilinogen synthase elucidate the structures of enzyme-bound product and a Schiff base intermediate.
Related Articles 15N and 13C NMR studies of ligands bound to the 280,000-dalton protein porphobilinogen synthase elucidate the structures of enzyme-bound product and a Schiff base intermediate.
Biochemistry. 1990 Sep 11;29(36):8345-50
Authors: Jaffe EK, Markham GD, Rajagopalan JS
Porphobilinogen synthase (PBGS) catalyzes the asymmetric condensation of two molecules of...
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08-21-2010 11:04 PM
[NMR paper] NMR studies of interactions of ligands with dihydrofolate reductase.
NMR studies of interactions of ligands with dihydrofolate reductase.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR studies of interactions of ligands with dihydrofolate reductase.
Biochem Pharmacol. 1990 Jul 1;40(1):141-52
Authors: Feeney J
NMR spectroscopy is a useful technique for studying interactions, conformations and dynamic processes within ligand-protein complexes. Several examples of the application of the method to studies of complexes of anti-folate...