contact

Dr. Christoph Rademacher
Dr. Christoph Rademacher
Group Leader
Phone:+49 331 567-9358

Max Planck Institute of Colloids and Interfaces, Am Mühlenberg 1, 14476 Potsdam

Structural Glycobiology

Room: 0.176

Structural Glycobiology

Structural Glycobiology

The  Research Group “Structural Glycobiology” has a strong focus on protein-ligand interactions using biophysical and computational techniques. In particular, we are interested in glycan-binding proteins, developing small molecular inhibitors as well as studying the recognition of their natural carbohydrate ligands. These findings are combined with functional studies of glycan-binding proteins in their native environment to foster our understanding of glycobiology in a structural context.

Research

The  Research Group “Structural Glycobiology” has a strong focus on protein-ligand interactions using biophysical and computational techniques. In particular, we are interested in glycan-binding proteins, developing small molecular inhibitors as well as studying the recognition of their natural carbohydrate ligands. These findings are combined with functional studies of glycan-binding proteins in their native environment to foster our understanding of glycobiology in a structural context. [more]
Dr. Christoph Rademacher, Dr. Robert Wawrzinek, Jessica Schulze, Hannes Baukmann, Felix Fuchsberger, <br />Hengxi Zhang, Mareike Rentzsch, <br />Jil Busmann, Nevena Mateva, <br />Benjamin Kurtze

Group Members

Dr. Christoph Rademacher, Dr. Robert Wawrzinek, Jessica Schulze, Hannes Baukmann, Felix Fuchsberger, 
Hengxi Zhang, Mareike Rentzsch, 
Jil Busmann, Nevena Mateva, 
Benjamin Kurtze [more]
<ol class="list">
<li>Aretz J. et al. (2017) Identification of Multiple Druggable Secondary Sites by Fragment Screening against DC-SIGN. Angew Chem Int Ed Engl. 56, 1-6</li>
<li>Glas A, Wamhoff EC et al. (2017) Increased Conformational Flexibility of a Macrocycle-Receptor Complex Contributes to Reduced Dissociation Rates. Chem. Eur. J., 23, 16157-61</li>
<li>Hanske J. et al. (2017) Bacterial polysaccharide specificity of the pattern recognition receptor Langerin is highly species dependent. J Biol Chem., 292, 862-871.</li>
<li>Hanske, J. et al. (2016) An intra-domain allosteric network modulates the calcium affinity of the C-type lectin receptor Langerin.  J Am Chem Soc 138, 12176-86.</li>
</ol>

Publications

  1. Aretz J. et al. (2017) Identification of Multiple Druggable Secondary Sites by Fragment Screening against DC-SIGN. Angew Chem Int Ed Engl. 56, 1-6
  2. Glas A, Wamhoff EC et al. (2017) Increased Conformational Flexibility of a Macrocycle-Receptor Complex Contributes to Reduced Dissociation Rates. Chem. Eur. J., 23, 16157-61
  3. Hanske J. et al. (2017) Bacterial polysaccharide specificity of the pattern recognition receptor Langerin is highly species dependent. J Biol Chem., 292, 862-871.
  4. Hanske, J. et al. (2016) An intra-domain allosteric network modulates the calcium affinity of the C-type lectin receptor Langerin.  J Am Chem Soc 138, 12176-86.
[more]
Drug Discovery Seminar<br />Glycobiology Lecture and Seminar

Teaching

Drug Discovery Seminar
Glycobiology Lecture and Seminar [more]
 
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