1k1f: Difference between revisions

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[[Image:1k1f.gif|left|200px]]
{{Seed}}
[[Image:1k1f.png|left|200px]]


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{{STRUCTURE_1k1f|  PDB=1k1f  |  SCENE=  }}  
{{STRUCTURE_1k1f|  PDB=1k1f  |  SCENE=  }}  


'''Structure of the Bcr-Abl Oncoprotein Oligomerization domain'''
===Structure of the Bcr-Abl Oncoprotein Oligomerization domain===




==Overview==
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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.
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{{ABSTRACT_PUBMED_11780146}}


==About this Structure==
==About this Structure==
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[[Category: Coiled coil]]
[[Category: Coiled coil]]
[[Category: Oligomerization]]
[[Category: Oligomerization]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:10:52 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 21:17:05 2008''

Revision as of 18:17, 1 July 2008

File:1k1f.png

Template:STRUCTURE 1k1f

Structure of the Bcr-Abl Oncoprotein Oligomerization domain

Template:ABSTRACT PUBMED 11780146

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

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