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1k1f
From Proteopedia
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[[Image:1k1f.gif|left|200px]] | [[Image:1k1f.gif|left|200px]] | ||
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'''Structure of the Bcr-Abl Oncoprotein Oligomerization domain''' | '''Structure of the Bcr-Abl Oncoprotein Oligomerization domain''' | ||
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[[Category: Malashkevich, V N.]] | [[Category: Malashkevich, V N.]] | ||
[[Category: Zhao, X.]] | [[Category: Zhao, X.]] | ||
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| - | [[Category: | + | [[Category: Oligomerization]] |
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Revision as of 19:10, 2 May 2008
Structure of the Bcr-Abl Oncoprotein Oligomerization domain
Overview
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.
About this Structure
1K1F is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of the Bcr-Abl oncoprotein oligomerization domain., Zhao X, Ghaffari S, Lodish H, Malashkevich VN, Kim PS, Nat Struct Biol. 2002 Feb;9(2):117-20. PMID:11780146 Page seeded by OCA on Fri May 2 22:10:52 2008
