1K1F

Structure of the Bcr-Abl Oncoprotein Oligomerization domain

Summary for 1K1F

• Entry DOI: 10.2210/pdb1k1f/pdb
• Descriptor: BREAKPOINT CLUSTER REGION PROTEIN (2 entities in total)
• Functional Keywords: oligomerization, coiled coil, bcr-abl kinase, transferase
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 8
• Total formula weight: 69675.50

Authors

Zhao, X.,Ghaffari, S.,Lodish, H.,Malashkevich, V.N.,Kim, P.S. (deposition date: 2001-09-25, release date: 2002-02-06, Last modification date: 2024-10-30)

Primary citation

Zhao, X.,Ghaffari, S.,Lodish, H.,Malashkevich, V.N.,Kim, P.S.
Structure of the Bcr-Abl oncoprotein oligomerization domain.
Nat.Struct.Biol., 9:117-120, 2002

PubMed 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.

PubMed: 11780146

Experimental method

X-RAY DIFFRACTION (2.2 Å)