1zzp

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Solution structure of the F-actin binding domain of Bcr-Abl/c-Abl

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

The Bcr-Abl tyrosine kinase causes different forms of leukemia in humans., Depending on its position within the cell, Bcr-Abl differentially affects, cellular growth. However, no structural and molecular details for the, anticipated localization determinants are available. We present the NMR, structure of the F-actin binding domain (FABD) of Bcr-Abl and its cellular, counterpart c-Abl. The FABD forms a compact left-handed four-helix bundle, in solution. We show that the nuclear export signal (NES) previously, reported in this region is part of the hydrophobic core and nonfunctional, in the intact protein. In contrast, we could identify the critical, residues of helix alphaIII that are responsible for F-actin binding and, cytoskeletal association. We propose that these interactions represent a, major determinant for both Bcr-Abl and c-Abl localization.

Disease

Known diseases associated with this structure: Leukemia, Philadelphia chromosome-positive, resistant to imatinib OMIM:[189980]

About this Structure

1ZZP is a Single protein structure of sequence from Homo sapiens. Active as Transferase, with EC number and 2.7.10.2 2.7.10.1 and 2.7.10.2 Full crystallographic information is available from OCA.

Reference

Structural basis for the cytoskeletal association of Bcr-Abl/c-Abl., Hantschel O, Wiesner S, Guttler T, Mackereth CD, Rix LL, Mikes Z, Dehne J, Gorlich D, Sattler M, Superti-Furga G, Mol Cell. 2005 Aug 19;19(4):461-73. PMID:16109371

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