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 |
| + | |PDB= 1k1f |SIZE=350|CAPTION= <scene name='initialview01'>1k1f</scene>, resolution 2.20Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''Structure of the Bcr-Abl Oncoprotein Oligomerization domain''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1K1F is a [ | + | 1K1F is a [[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== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11780146 11780146] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: oligomerization]] | [[Category: oligomerization]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:11:12 2008'' |
Revision as of 10:11, 20 March 2008
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| , resolution 2.20Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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