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Structure of Telomerase RNA and telomeric proteins


EMSL Project ID
10295c

Abstract

We are using NMR to study the structure/function relationship of human telomerase, the ribonucleoprotein (RNP) enzyme responsible in most eukaryotes for the replication of the chromosome termini (telomeres). Since it is selectively activated in most human cancers, its inhibition could provide new antineoplastic agents with broad activity. Despite its importance, there are at the moment only a few high-resolution structures for the protein components of telomerase or the essential structural domains of its RNA component. This is a critical limitation in efforts directed at addressing the biological function of this enzyme. More specifically, we are studying the structure of two critical domains of human telomerase RNA responsible respectively for RNA biogenesis and for recruitment of the catalytic activity to the holoenzyme and the proteins that interact with these RNA domains. Because we ultimately aim to use this information for drug design, the quality of the structure is of the utmost importance. Access to the highest available field, as provided by EMSL, is therefore essential.

Project Details

Project type
Capability Research
Start Date
2006-04-04
End Date
2007-05-21
Status
Closed

Team

Principal Investigator

Gabriele Varani
Institution
University of Washington

Team Members

Darren Begley
Institution
Emerald BioStructures

Bradley Lunde
Institution
University of Washington

Thomas Leeper
Institution
University of Washington