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Printable Handouts
Navigable Slide Index
- Introduction
- Protein-glycan interactions
- Reasons for new methodology
- Chemokine CCL5 interactions with GAGs
- Crystal structure of a CCL5 dimer
- NMR provides ligand binding information
- STD-NOESY of 444 complex
- Building models with a ligand
- NMR works well for studies of smaller systems
- Residual dipolar coupling (RDC)
- WT CCL5 at low pH
- RDC data for E66S and WT CCL5
- Multiple models for the tetramer structure
- SAXS data yield additional shape restrictions
- Fixing dimer orientations
- Cross-saturation confirms interface residues
- MS hydroxyl radical footprinting
- Radical footprinting & NMR cross-saturation
- Tetramer model extends to higher oligomers
- Modeling in longer GAG oligomers
- Glycans on a glycoprotein
- Why do we care about IgG glycosylation?
- How do glycans modulate receptor interactions?
- Glycans on native IgG-Fc are very heterogeneous
- Investigating differential branch accessibility
- Preparing IgG with homogeneous 13C glycans (1)
- Production of 13C labeled IgG-Fc fragment
- 1-3 branch is mobile and 1-6 branch is restrained
- Relaxation dispersion probes slow exchange
- Relaxation dispersion and chemical shift data
- Model for galactose terminated Fc glycans
- Locating glycans more precisely
- Predicted distances based on 1IGT structure
- Gal PREs in the Dy+++ : Z-L2LBT: Fc complex
- Sialylated glycans and rheumatoid arthritis
- Sialic acid can be produced in a labeled form
- Preparing IgG with homogeneous 13C glycans (2)
- 13C-Gal labeled Fc + & - sialic acid
- Sialic acid addition & observation of NMR spectra
- CPMG R2 relaxation can be measured
- Di-sialylation & shift to glycan-exposed state
- Summary
- Acknowledgments
Topics Covered
- NMR studies
- Protein structure
- Protein-protein Interactions
- Building models with a ligand
- Chemokine CCL5 interactions with GAGs
- STD-NOESY
- Residual dipolar coupling (RDC)
- SAXS data
- Cross-saturation
- Radical footprinting
- Glycans on a glycoprotein
- - Preparing IgG with homogeneous 13C glycans
- Relaxation dispersion
- Galactose terminated Fc glycans Locating glycans more precisely
- Sialylated glycans
- CPMG R2 relaxation
- Di-sialylation
Talk Citation
Prestegard, J. (2012, November 27). Protein-glycan interactions [Video file]. In The Biomedical & Life Sciences Collection, Henry Stewart Talks. Retrieved November 9, 2024, from https://doi.org/10.69645/YHGU1308.Export Citation (RIS)
Publication History
Financial Disclosures
- Prof. James Prestegard has not informed HSTalks of any commercial/financial relationship that it is appropriate to disclose.