2LK4

Structural and mechanistic insights into the interaction between PAT Pyk2 and Paxillin LD motif

2LK4 の概要

• エントリーDOI: 10.2210/pdb2lk4/pdb
• NMR情報: BMRB: 17974
• 分子名称: Protein-tyrosine kinase 2-beta (1 entity in total)
• 機能のキーワード: transferase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: Q14289
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14815.05

構造登録者

Vanarotti, M.,Miller, D.,Guibao, C.,Zheng, J. (登録日: 2011-10-04, 公開日: 2012-10-10, 最終更新日: 2024-05-01)

主引用文献

Vanarotti, M.S.,Miller, D.J.,Guibao, C.D.,Nourse, A.,Zheng, J.J.
Structural and Mechanistic Insights into the Interaction between Pyk2 and Paxillin LD Motifs.
J.Mol.Biol., 426:3985-4001, 2014

PubMed Abstract: Proline-rich tyrosine kinase 2 (Pyk2) is a member of the focal adhesion kinase (FAK) subfamily of cytoplasmic tyrosine kinases. The C-terminal Pyk2-focal adhesion targeting (FAT) domain binds to paxillin, an adhesion molecule. Paxillin has five leucine-aspartate (LD) motifs (LD1-LD5). Here, we show that the second LD motif of paxillin, LD2, interacts with Pyk2-FAT, similar to the known Pyk2-FAT/LD4 interaction. Both LD motifs can target two ligand binding sites on Pyk2-FAT. Interestingly, they also share similar binding affinity for Pyk2-FAT with preferential association to one site relative to the other. Nevertheless, the LD2-LD4 region of paxillin (paxillin(133-290)) binds to Pyk2-FAT as a 1:1 complex. However, our data suggest that the Pyk2-FAT and paxillin complex is dynamic and it appears to be a mixture of two distinct conformations of paxillin that almost equally compete for Pyk2-FAT binding. These studies provide insight into the underlying selectivity of paxillin for Pyk2 and FAK that may influence the differing behavior of these two closely related kinases in focal adhesion sites.

PubMed: 25174335
DOI: 10.1016/j.jmb.2014.08.014

実験手法

SOLUTION NMR