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Glycoprotein structural genomics: solving the glycosylation problem.

Veronica T Chang1, Max Crispin, A Radu Aricescu

  • 1Nuffield Department of Clinical Medicine and MRC Human Immunology Unit, Weatherall Institute of Molecular Medicine, University of Oxford, Oxford OX3 9DS, United Kingdom.

Structure (London, England : 1993)
|March 16, 2007
PubMed
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Structural genomics faces challenges with glycoproteins. This study introduces a method using N-glycosylation inhibitors in mammalian cells to improve glycoprotein crystallization for structural analysis.

Area of Science:

  • Structural Biology
  • Glycobiology
  • Genomic Analysis

Background:

  • Glycoproteins require correct glycosylation for proper folding.
  • Heterogeneity in glycoproteins often hinders crystallization for structural studies.

Purpose of the Study:

  • To address the challenges in structural genomic analysis of glycoproteins.
  • To develop a method for enhancing glycoprotein crystallization.

Main Methods:

  • Transient expression of glycoproteins in mammalian cells.
  • Inhibition of N-glycosylation processing using kifunensine or swainsonine.
  • Enzymatic treatment with endoglycosidase H to simplify N-glycans.

Main Results:

  • The method allows correct glycoprotein folding while maintaining sensitivity to enzymatic modification.

Related Experiment Videos

  • N-glycans are reduced to single residues, significantly enhancing crystallization potential.
  • Scalability of transient mammalian expression is comparable to bacterial systems.

    • Conclusions:

    • This approach effectively solves the 'glycosylation problem' in structural genomics.
    • It overcomes a major bottleneck in determining glycoprotein structures.
    • The method facilitates structural genomic analysis by improving crystallization of complex glycoproteins.