Abstract

Vinculin is large protein of MW 120 KDa, of unknown structure, which plays a central role in the assembly of focal adhesions. These are macromoleular complexes found at cell-matrix junctions, which provide a structural and functional link between the extracellular matrix and the actin cytoskeleton. Much is known about the binding activities of vinculin in vitro, and the field is well poised to benefit from structural data at atomic resolution, which would elucidate the structural basis of focal adhesion assembly and regulation

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Cooperative Agreements (U41)
Project #
5U41RR007707-10
Application #
6483549
Study Section
Project Start
2001-08-15
Project End
2002-08-14
Budget Start
1997-10-01
Budget End
1998-09-30
Support Year
10
Fiscal Year
2001
Total Cost
$120,630
Indirect Cost

  Institution

Name
University of Chicago
Department
Type
DUNS #
225410919
City
Chicago
State
IL
Country
United States
Zip Code
60637

  Publications

Durbin, S M; Clevenger, T; Graber, T et al. (2012) X-ray pump optical probe cross-correlation study of GaAs. Nat Photonics 6:111-114
Neutze, Richard; Moffat, Keith (2012) Time-resolved structural studies at synchrotrons and X-ray free electron lasers: opportunities and challenges. Curr Opin Struct Biol 22:651-9
Horsman, Geoff P; Ke, Jiyuan; Dai, Shaodong et al. (2006) Kinetic and structural insight into the mechanism of BphD, a C-C bond hydrolase from the biphenyl degradation pathway. Biochemistry 45:11071-86