Molecular chaperones play key roles in protein folding, transport across membranes, and in response to stressful stimuli. Hsc20 is a DnaJ-type """"""""co-chaperone"""""""" protein encoded in a recently discovered operon in E. coli which also encodes a DnaK/hsp70-type chaperone. To date, no structure for a DnaJ co-chaperone has been determined. We have recently succeeded in overexpresing, purifying and crystallizing Hsc20. Thus, Hsc20 could provide the first complete high resolution crystal structure for proteins of this class.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR001209-22
Application #
6437542
Study Section
Project Start
2001-03-01
Project End
2002-02-28
Budget Start
Budget End
Support Year
22
Fiscal Year
2001
Total Cost
$143,176
Indirect Cost
Name
Stanford University
Department
Type
DUNS #
800771545
City
Stanford
State
CA
Country
United States
Zip Code
94305
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