We examined the structure of the myosin light chain domain in three known conformational states. A combination of crystallographic and electron microscopic results from the literature, and our own spectroscopic experiments, were combined to elucidate myosin's conformation in various biochemical states. Using the resources of the Computer Graphics Laboratory, we determined that the two light chain domains of a single myosin molecule were separated by a minimum of ~80 angstroms when both heads are bound to actin in strongly-bound states. This placed important constraints on our data, and allowed us to construct a novel model for force maintenance and the latch state in smooth muscle.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR001081-23
Application #
6347870
Study Section
Project Start
2000-07-01
Project End
2001-06-30
Budget Start
1998-10-01
Budget End
1999-09-30
Support Year
23
Fiscal Year
2000
Total Cost
$7,632
Indirect Cost
Name
University of California San Francisco
Department
Type
DUNS #
073133571
City
San Francisco
State
CA
Country
United States
Zip Code
94143
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