This subproject is one of many research subprojects utilizing theresources provided by a Center grant funded by NIH/NCRR. The subproject andinvestigator (PI) may have received primary funding from another NIH source,and thus could be represented in other CRISP entries. The institution listed isfor the Center, which is not necessarily the institution for the investigator.Dynein binds to microtubules via a long antiparallel coiled coil with a 6 helix domain at the tip. Binding of ATP to the head of the dynein is likely to be communicated to the microtubule binding domain (MTBD) along the coiled coil and how this occurs is likely to be very interesting from a structural perspective. We have fused the MTBD and part of the stalk to the coiled coil found on seryl-tRNA synthetase. My collaborator has shown that be varying the site of fusion we can modulate the affinity of the MTBD for microtubules. We now have crystals of one of these constructs (the weak binding form).

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR001209-29
Application #
7722090
Study Section
Special Emphasis Panel (ZRG1-BPC-E (40))
Project Start
2008-03-01
Project End
2009-02-28
Budget Start
2008-03-01
Budget End
2009-02-28
Support Year
29
Fiscal Year
2008
Total Cost
$573
Indirect Cost
Name
Stanford University
Department
Chemistry
Type
Schools of Arts and Sciences
DUNS #
009214214
City
Stanford
State
CA
Country
United States
Zip Code
94305
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