1ZZP

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

1ZZP の概要

• エントリーDOI: 10.2210/pdb1zzp/pdb
• NMR情報: BMRB: 6570
• 分子名称: Proto-oncogene tyrosine-protein kinase ABL1 (1 entity in total)
• 機能のキーワード: four helix bundle, nuclear export signal, transferase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm, cytoskeleton. Isoform IB: Nucleus membrane; Lipid-anchor: P00519
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14150.12

構造登録者

Hantschel, O.,Wiesner, S.,Guttler, T.,Mackereth, C.D.,Rix, L.L.R.,Mikes, Z.,Dehne, J.,Gorlich, D.,Sattler, M.,Superti-Furga, G. (登録日: 2005-06-14, 公開日: 2005-08-30, 最終更新日: 2024-05-22)

主引用文献

Hantschel, O.,Wiesner, S.,Guttler, T.,Mackereth, C.D.,Rix, L.L.R.,Mikes, Z.,Dehne, J.,Gorlich, D.,Sattler, M.,Superti-Furga, G.
Structural Basis for the Cytoskeletal Association of Bcr-Abl/c-Abl.
Mol.Cell, 19:461-473, 2005

PubMed Abstract: 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.

PubMed: 16109371
DOI: 10.1016/j.molcel.2005.06.030

実験手法

SOLUTION NMR