1k1f
From Proteopedia
(New page: 200px<br /> <applet load="1k1f" size="450" color="white" frame="true" align="right" spinBox="true" caption="1k1f, resolution 2.20Å" /> '''Structure of the Bc...) |
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| - | [[Image:1k1f.gif|left|200px]]<br /> | + | [[Image:1k1f.gif|left|200px]]<br /><applet load="1k1f" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1k1f" size=" | + | |
caption="1k1f, resolution 2.20Å" /> | caption="1k1f, resolution 2.20Å" /> | ||
'''Structure of the Bcr-Abl Oncoprotein Oligomerization domain'''<br /> | '''Structure of the Bcr-Abl Oncoprotein Oligomerization domain'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The Bcr-Abl oncoprotein is responsible for a wide range of human | + | 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. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1K1F is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1K1F is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K1F OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Ghaffari, S.]] | [[Category: Ghaffari, S.]] | ||
| - | [[Category: Kim, P | + | [[Category: Kim, P S.]] |
[[Category: Lodish, H.]] | [[Category: Lodish, H.]] | ||
| - | [[Category: Malashkevich, V | + | [[Category: Malashkevich, V N.]] |
[[Category: Zhao, X.]] | [[Category: Zhao, X.]] | ||
[[Category: bcr-abl kinase]] | [[Category: bcr-abl kinase]] | ||
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[[Category: oligomerization]] | [[Category: oligomerization]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:29:13 2008'' |
Revision as of 11:29, 21 February 2008
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Structure of the Bcr-Abl Oncoprotein Oligomerization domain
Contents |
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.
Disease
Known diseases associated with this structure: Leukemia, acute lymphocytic OMIM:[151410], Leukemia, chronic myeloid OMIM:[151410]
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 Thu Feb 21 13:29:13 2008
