The 3-dimensional structure of the wild type R subunit will provide important information on how the two monomers are relatively oriented to each other, how the protein dimerizies and how the hinge region folds, which is totally disordered in the deletion mutant structure. This dimerization domain also provides a docking site for anchoring the holoenzyme to a variety of scaffolding proteins both in cytoplasm and the nucleus. The crystals of mutant R subunits have defects in their cAMP binding sites. Their structures at high resolution are essential for defining the molecular features of these cAMP binding sites and for understanding the conformational changes which are induced by cAMP binding.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR001209-22
Application #
6437643
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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