Jennifer Kavran Graduate Student Center for Structural Biology Department of Molecular Biophysics & Biochemistry Yale University 266 Whitney Avenue, 413 Bass Center New Haven, CT 06520-8114 Phone:  (203) 432-5627 FAX:  (203) 432-3282 Email:   kavran [ at ] csb.yale.edu

Summary:

Proper Targeting of nascent proteins to their final destination is essential for cellular function. Signal sequence bearing polypeptides are bound by the signal sequence recognition particle (SRP) as they emerge from the exit tunnel on the large ribosomal subunit. Recognition of the signal sequence in Eukarya is concomitant with the elongation arrrest of the nascent protein. SRP then delivers the nascent polypeptide/ribosome complex to the membrane where it is fed through an aqueous pore, the translocon, either to be secreted or integrated into the bilayer (1). Our goal is to determine a high resolution X-ray crystal structure of an SRP-ribosome complex. These structural results will allow us to determine the recognition elements for the SRP/ribosome complex, the mechanism of elongation arrest, and the structure of the SRP particle.
  References:

(1) Kennan, R.J., Freymann, D.M., Stroud, R.M., and Walter, P. (2001) Annu. Re v. Biochem. 70, 755-75.