1k1f

From Proteopedia

proteopedia linkproteopedia link

spinqualitylabelsall models 1k1f, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Structure of the Bcr-Abl Oncoprotein Oligomerization domain

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

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 Mon Nov 12 17:46:31 2007