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Structure, Vol. 12, 10871097, June, 2004, 2004 Elsevier Ltd. All rights reserved. DOI 10.1016/j.str.2004.03.020 The Crystal Structure of the Carboxy-Terminal
 

Summary: Structure, Vol. 12, 10871097, June, 2004, 2004 Elsevier Ltd. All rights reserved. DOI 10.1016/j.str.2004.03.020
The Crystal Structure of the Carboxy-Terminal
Dimerization Domain of htpG, the Escherichia coli
Hsp90, Reveals a Potential Substrate Binding Site
Neckers, 2002). Variation in Hsp90 function has also
been realized as a molecular mechanism underlying
evolution (Rutherford and Lindquist, 1998; Queitsch et
al., 2002). In sum, this ubiquitous chaperone impacts a
wealth of processes over a huge range of both biological
Seth F. Harris, Andrew K. Shiau,
and David A. Agard*
The Howard Hughes Medical Institute and
The Department of Biochemistry and Biophysics
University of California, San Francisco
San Francisco, California 94143 themes and time scales, influencing molecular events
with fluctuations on the order of seconds while also
helping to shape organisms over the passage of eons.
The ongoing discovery of the biological roles of Hsp90Summary
has outpaced elucidation of the molecular mechanisms
underlying its function. The protein contains three majorHsp90 is a ubiquitous, well-conserved molecular

  

Source: Agard, David - Department of Biochemistry and Biophysics, University of California at San Francisco

 

Collections: Biotechnology; Biology and Medicine