Jeffrey L. Hansen, Ph.D.
                      Assistant  Professor
     
  2003 Assistant Professor, Medical University of South Carolina, Charleston, SC
  2001 Associate Research Scientist, Yale University, New Haven, CT
  1997-2001 Postdoctoral Researcher, Yale University, New Haven, CT
  1991-1997 Ph.D., Chemistry, University of Colorado, Boulder, CO
  1986-1990 B.S., Biochemistry, Old Dominion University, Norfolk, VA
     
     
     



Office: 843-792-7773
Lab: 843-792-8226
Fax: 843-792-1627
Email: hansenjl@musc.edu
BSB-535E
 
 

Research Interests
 

Our lab uses x-ray crystallography to study complexes that form between RNA molecules and proteins. Our goal is gain insights into disease-causing mechanisms. We plan to use atomic resolution structures as a basis to design new therapeutics.

RNA/protein complexes are at the center of life’s most fundamental processes. It is not surprising that problems within these complexes cause many diseases. Therefore, many therapeutics are designed to target RNA/protein complexes. For example, the ribosome is the RNA/protein complex that makes proteins in the cell. Ribosomes make proteins by aligning codons in messenger RNA (mRNA) with anticodons in transfer RNA (tRNA) and then catalyzing peptide bond formation. Because life can be sustained only by continuous protein translation, most clinically useful antibiotics kill bacterial by targeting their ribosomes. A dozen atomic resolution x-ray crystal structures of the ribosome have been solved since the year 2000 (see publications below). These structures show in atomic detail how various antibiotics bind to the ribosome, how antibiotics kill bacteria, and how mutations in bacterial ribosomes confer resistance to antibiotics. Currently, these structures are being used as a basis to design new antibiotics to kill bacteria that have become resistant to existing antibiotics.

Our lab is now applying the same approach to study a different RNA/protein complex, telomerase. Telomerase is involved in aging and in cancer. The abnormal function of telomerase is required by most cancer cells in order to become immortal. We are testing several approaches in our effort to gain structural information on telomerase or on proteins involved in telomerase biogenesis. We plan to use this information to develop cancer therapeutics that target telomerase activity.

 

Selected Publications