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Collaborative X-ray Crystallography Group

3-Dimensional Characterization

Lars C. Pedersen, Ph.D.
Group Leader

Tel (919) 541-0444
Fax (919) 541-7880
pederse2@niehs.nih.gov

Curriculum Vitae  (57KB)

P.O. Box 12233
Mail Drop F3-09
Research Triangle Park, North Carolina 27709
Delivery Instructions

Research Summary

The main objective of the Collaborative X-ray Crystallography Group in the Laboratory of Structural Biology (LSB) is to provide a resource to the NIEHS community that allows for 3-dimensional structural characterization using molecular biology, biochemistry and X-ray crystallographic techniques on biological systems of interest-protein/ligand, oligonucleotides, protein/oligonucleotides or protein/protein.

Over the last few years, main areas of research have been focused on heparan sulfate/heparin biosynthesis, DNA repair, and the study of allergens, but the focus continuously changes to meet the needs of NIEHS investigators.

Major areas of research:

• Heparan Sulfate/heparin biosynthesis — Sulfation at specific hydroxyls and amines along the polysaccharide chain confers specificity for heparan sulfate binding in various processes such as organogenesis, blood coagulation, growth factor/cytokine action, lipid metabolism, and viral infection. The sulfation along the heparan sulfate chain is carried out by individual sulfotransferases that recognize specific target. We are interested in understanding the substrate recognition of these enzymes for use in drug synthesis using a chemoenzymatic process.
• DNA repair — In support of research conducted in the Wilson lab and Kunkel lab, we have been studying the X-family polymerases β and λ to understand their roles in DNA repair processes such as base excision repair and non-homologous end joining.
• Allergen Studies — In support of research conducted in the London lab, we have been studying crystal structures of allergens from dust mites (Der p 5 and Der p 7) as well as the major peanut allergen Ara h 2 to better understand how they elicit an immune response.

Binding of a heptasaccharide to 3-O-sulfotransferase-1. Sulfation of this substrate produces heparin sulfate with anti-coagulant activity.

The crystal structure of Ara h 2 (green) was obtained as a fusion molecule with the maltose protein (magenta).

Lars C. Pedersen, Ph.D., heads the Collaborative X-ray Crystallography Group within the LSB. Pedersen is also an Adjunct Associate Professor in the Division of Pharmacotherapy and Experimental Therapeutics at the University of North Carolina at Chapel Hill School of Pharmacy. He received his Ph.D. in biochemistry from the University of Washington in Seattle in 1994, and has published over 70 peer-reviewed articles in leading biomedical journals. Pedersen joined the NIEHS in 1996 as a postdoctoral fellow in the laboratory of Masahiko Negishi, Ph.D., in the Laboratory of Reproductive and Developmental Toxicology. He started the Structure & Function Research Group in the LSB in 2002.

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