BNL Biology
Biology Department
Brookhaven National Laboratory

Catherine L. Lawson
Ph.D. 1987 University of Chicago

Biology Department, 463
Brookhaven National Laboratory
Upton, NY 11973-5000

current address:

Department of Chemistry
Rutgers University
610 Taylor Road
Piscataway, NJ 08854

tel: (732) 445-2602
fax: (732) 445-5312
lawson@rutchem.rutgers.edu

Research Interests:

Crystallographic methods are being used to determine the three-dimensional structures of selected proteins in order to investigate structure/function relationships. Our two active areas of research are (1) surface antigens of the Lyme disease spirochete, Borrelia burgdorferi, and (2) lentivirus gag components.

Antigenic proteins from Borrelia burgdorferi (the Lyme disease spirochete) and related organisms are under investigation to determine protein folds for use in rational vaccine design.
Image: Crystals of B. burgdorferi OspA complexed with Fab fragment of protective antibody LA-2.

The recently completed structure of EIAV p26 capsid protein (EIAV = equine infectious anemia virus, a lentivirus related to HIV) suggests how the protein assembles into an impenetrable shell to protect the viral RNA genome.
Image: Molecular handshake between EIAV p26 subunits is carried out by their C-terminal domains.

The unique OspA structure is on the cover of the BNL staff manual.
To view the full length of its 21-stranded beta sheet click on the icon.

Lyme Disease Antigen References:
 
  • Li, H., Dunn, J.J., Luft, B.J. and Lawson, C.L.,
    Crystal structure of Lyme disease antigen OspA complexed with an Fab.
    Proc. Natl. Acad. Sci. USA, 94, 3584-3589 (1997). Medline Abstract; Full Text (pdf)
  • Li, H. and Lawson, C.L.,
    Crystallization and preliminary X-ray analysis of Borrelia burgdorferi outer surface protein A (OspA) complexed with a murine monoclonal antibody Fab fragment.
    J. Struct. Biol. 115, 335-337 (1995). Medline Abstract

Trp repressor mini-movie!:
This simple gif movie shows the L-tryptophan binding site of trp repressor, which sits in the interface between two protein subunits (magenta and green). Only the region surrounding the ligand binding site is shown. Notice that only the + L-tryptophan state of the protein forms a surface complementary to the DNA backbone. Without L-tryptophan the magenta subunit collapses towards the green subunit. An Arginine side-chain moves to take the place of the L-tryptophan.

Selected trp Repressor References:
  • Lawson, C.L.,
    An atomic view of the L-tryptophan binding pocket of trp repressor.
    Nat. Struct. Biol. 3, 986-987 (1996). Medline Abstract; Full Text
  • Lawson, C.L.,
    Structural consequences of two methyl additions in the E. coli trp repressor L-tryptophan binding pocket.
    Proceedings of the 9th Convention in Biolmolecular Stereodynamics, Adenine Press, Schenectady, NY, pp 83-90, (1996). Abstract
  • Lawson, C.L.,
    A modified Crowther and Blow T1 translation function for partial search models.
    Acta Cryst. D51, 853-855 (1995).
  • Lawson, C.L., and Carey, J.,
    Tandem binding in crystals of a trp repressor/operator half-site complex.
    Nature, 366, 178-182 (1993). Medline Abstract

Lawson Lab News::

First students to graduate from the Lawson lab: Zhongmin Jin and Wei Ding in their regalia, May 1998

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