13C-labeled heparan sulfate analogue as a tool to study protein/heparan sulfate interaction by NMR spectroscopy. Application to the CXCL12? chemokine.
J Am Chem Soc. 2011 Jun 2;
Authors: Laguri C, Sapay N, Simorre JP, Brutscher B, Imberty A, Gans P, Lortat-Jacob H
Heparan sulfate, a polysaccharide of the glycosaminoglycan family characterized by a unique level of complexity, has emerged as a key regulator of many fundamental biological processes. Although it has become clear that this class of molecules exerts its functions by interacting with proteins, the exact modes of interaction still remain largely unknown. Here we report the engineering of a 13C-labeled heparan sulfate-like oligosaccharide with a defined oligosaccharidic sequence that is used to investigate the structural determinants involved in protein-heparan sulfate recognition by multidimensional NMR spectroscopy. Using the chemokine CXCL12? as a model system, we demonstrate how experimental NMR data obtained on both the oligosaccharide and the chemokine can be used to obtain a structural model of a protein-heparan sulfate complex. This new approach provides a foundation for further investigations of protein-HS interactions and should have wide applications.
PMID: 21634378 [PubMed - as supplied by publisher]
13C-Labeled Heparan Sulfate Analogue as a Tool To Study Protein/Heparan Sulfate Interactions by NMR Spectroscopy: Application to the CXCL12? Chemokine
13C-Labeled Heparan Sulfate Analogue as a Tool To Study Protein/Heparan Sulfate Interactions by NMR Spectroscopy: Application to the CXCL12? Chemokine
Ce?dric Laguri, Nicolas Sapay, Jean-Pierre Simorre, Bernhard Brutscher, Anne Imberty, Pierre Gans and Hugues Lortat-Jacob
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja201753e/aop/images/medium/ja-2011-01753e_0006.gif
Journal of the American Chemical Society
DOI: 10.1021/ja201753e
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA...
nmrlearner
Journal club
0
06-09-2011 01:32 AM
[NMR paper] Interaction between the type-3 copper protein tyrosinase and the substrate analogue p
Interaction between the type-3 copper protein tyrosinase and the substrate analogue p-nitrophenol studied by NMR.
Related Articles Interaction between the type-3 copper protein tyrosinase and the substrate analogue p-nitrophenol studied by NMR.
J Am Chem Soc. 2005 Jan 19;127(2):567-75
Authors: Tepper AW, Bubacco L, Canters GW
The interaction of the monooxygenating type-3 copper enzyme Tyrosinase (Ty) from Streptomyces antibioticus with its inhibitor p-nitrophenol (pnp) was studied by paramagnetic NMR methods. The pnp binds to oxidized Ty...
nmrlearner
Journal club
0
11-24-2010 11:14 PM
[NMR paper] Interaction between an amantadine analogue and the transmembrane portion of the influ
Interaction between an amantadine analogue and the transmembrane portion of the influenza A M2 protein in liposomes probed by 1H NMR spectroscopy of the ligand.
Related Articles Interaction between an amantadine analogue and the transmembrane portion of the influenza A M2 protein in liposomes probed by 1H NMR spectroscopy of the ligand.
J Med Chem. 2004 Sep 23;47(20):4975-8
Authors: Kolocouris A, Hansen RK, Broadhurst RW
1H NMR spectroscopy of a fluoroamantadine ligand was used to probe the pH dependence of binding to the transmembrane peptide...
nmrlearner
Journal club
0
11-24-2010 10:01 PM
[NMR paper] NMR structure of human apolipoprotein C-II in the presence of sodium dodecyl sulfate.
NMR structure of human apolipoprotein C-II in the presence of sodium dodecyl sulfate.
Related Articles NMR structure of human apolipoprotein C-II in the presence of sodium dodecyl sulfate.
Biochemistry. 2001 May 8;40(18):5414-21
Authors: MacRaild CA, Hatters DM, Howlett GJ, Gooley PR
The structure and protein-detergent interactions of apolipoprotein C-II (apoC-II) in the presence of SDS micelles have been investigated using circular dichroism and heteronuclear NMR techniques applied to (15)N-labeled protein. Micellar SDS, a commonly used...
nmrlearner
Journal club
0
11-19-2010 08:32 PM
[NMR paper] Porcine cerebroside sulfate activator (saposin B) secondary structure: CD, FTIR, and
Porcine cerebroside sulfate activator (saposin B) secondary structure: CD, FTIR, and NMR studies.
Related Articles Porcine cerebroside sulfate activator (saposin B) secondary structure: CD, FTIR, and NMR studies.
Mol Genet Metab. 1998 Jan;63(1):14-25
Authors: Waring AJ, Chen Y, Faull KF, Stevens R, Sherman MA, Fluharty AL
Cerebroside sulfate activator protein (CSAct or saposin B) is one of a group of heat stable, low-molecular-weight proteins that appear to share a common structural motif. These have been referred to as saposin-like proteins...
nmrlearner
Journal club
0
11-17-2010 11:06 PM
[NMR paper] Partial purification and substrate specificity of heparan sulfate alpha-N-acetylgluco
Partial purification and substrate specificity of heparan sulfate alpha-N-acetylglucosaminyltransferase I: synthesis, NMR spectroscopic characterization and in vitro assays of two aryl tetrasaccharides.
Related Articles Partial purification and substrate specificity of heparan sulfate alpha-N-acetylglucosaminyltransferase I: synthesis, NMR spectroscopic characterization and in vitro assays of two aryl tetrasaccharides.
Glycobiology. 1997 Jul;7(5):587-95
Authors: Fritz TA, Agrawal PK, Esko JD, Krishna NR
Studies of heparan sulfate biosynthesis...
nmrlearner
Journal club
0
08-22-2010 03:31 PM
[NMR paper] Partial purification and substrate specificity of heparan sulfate alpha-N-acetylgluco
Partial purification and substrate specificity of heparan sulfate alpha-N-acetylglucosaminyltransferase I: synthesis, NMR spectroscopic characterization and in vitro assays of two aryl tetrasaccharides.
Related Articles Partial purification and substrate specificity of heparan sulfate alpha-N-acetylglucosaminyltransferase I: synthesis, NMR spectroscopic characterization and in vitro assays of two aryl tetrasaccharides.
Glycobiology. 1997 Jul;7(5):587-95
Authors: Fritz TA, Agrawal PK, Esko JD, Krishna NR
Studies of heparan sulfate biosynthesis...
nmrlearner
Journal club
0
08-22-2010 03:03 PM
[NMR paper] Location of M13 coat protein in sodium dodecyl sulfate micelles as determined by NMR.
Location of M13 coat protein in sodium dodecyl sulfate micelles as determined by NMR.
Related Articles Location of M13 coat protein in sodium dodecyl sulfate micelles as determined by NMR.
Biochemistry. 1994 Nov 8;33(44):12990-7
Authors: Papavoine CH, Konings RN, Hilbers CW, van de Ven FJ
The major coat protein (gVIIIp) of bacteriophage M13 solubilized in sodium dodecyl sulfate (SDS) detergent micelles was used as a model system to study this protein in the lipid-bound form. In order to probe the position of gVIIIp relative to the SDS...