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- Title
Structure of the Bcr-Abl oncoprotein oligomerization domain.
- Authors
Zhao, Xun; Ghaffari, Saghi; Lodish, Harvey; Malashkevich, Vladimir N; Kim, Peter S
- Abstract
The Bcr-Abl oncoprotein is responsible for a wide range of human leukemias, including most cases of Philadelphia chromosome-positive chronic myelogenous leukemia. Oligomerization of Bcr-Abl is essential for oncogenicity. We determined the crystal structure of the N-terminal oligomerization domain of Bcr-Abl (residues 1-72 or Bcr1-72) and found a novel mode of oligomer formation. Two N-shaped monomers dimerize by swapping N-terminal helices and by forming an antiparallel coiled coil between C-terminal helices. Two dimers then stack onto each other to form a tetramer. The Bcr1-72 structure provides a basis for the design of inhibitors of Bcr-Abl transforming activity by disrupting Bcr-Abl oligomerization.
- Publication
Nature structural biology, 2002, Vol 9, Issue 2, p117
- ISSN
1072-8368
- Publication type
Journal Article
- DOI
10.1038/nsb747