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GeNMR
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Fragment-based:
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Refinement:
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Structure from chemical shifts:
Fragment-based:
WeNMR CS-Rosetta
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Homology-based:
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Torsion angles from chemical shifts:
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Secondary structure from chemical shifts:
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Flexibility from chemical shifts:
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Interactions from chemical shifts:
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Chemical shifts re-referencing:
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Molecular dynamics:
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From structure:
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From sequence:
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Disordered proteins:
MAXOCC
Format conversion & validation:
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From NMR-STAR 3.1
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NMR sample preparation:
Protein disorder:
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Protein solubility:
camLILA
ccSOL
Camfold
camGroEL
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Isotope labeling:
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Solid-state NMR:
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Default 13C-labeled heparan sulfate analogue as a tool to study protein/heparan sulfate interaction by NMR spectroscopy. Application to the CXCL12? chemokine.

13C-labeled heparan sulfate analogue as a tool to study protein/heparan sulfate interaction by NMR spectroscopy. Application to the CXCL12? chemokine.

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]



Source: PubMed
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