Small-angle scattering data from type Ia cGMP-dependent protein kinase (PKG) titrated with cGMP (1 through 13 molar equivalents) shows a large conformational change induced by cGMP-binding. PKG is a dimer with a regulatory and catalytic domain within each monomer component. There is one 'slow' and one 'fast' cGMP binding site on each monomer. A P(r) analysis of the scattering data indicates that the conformational change involves a shift of the molecular mass away from the center of the molecule, possibly due to the movement of the regulatory domain away from the catalytic domain. The radius of gyration of PKG increases dramatically by 30% from 45.4 to 59.4 E upon addition of cGMP. It appears that the 4 cGMP binding sites per PKG may only need to be partially saturated to see the full confromational change. Further study is underway to characterize the exact role of the slow and fast cGMP-binding sites.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR001209-22
Application #
6437711
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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