Myosin light chain kinase binding to actin filaments

FEBS Letters

Stull, James T¹  Smith, Lula¹ 

[1] Department of Physiology, The University of Texas Southwestern Medical Center at Dallas, 5323 Harry Hines Boulevard, Dallas, TX 75390-9040, USA

关键词: Myosin light chain kinase;    Myofilament;    Actin;    Calmodulin;    Calcium;    MLCK;    myosin light chain kinase;    CaM;    calmodulin;    MOPS;    3-(N-morpholino)propanesulfonic acid;    GST;    glutathione S-transferase;   

DOI  :  10.1016/S0014-5793(00)01931-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Smooth muscle myosin light chain kinase (MLCK) plays important roles in contractile-motile processes of a variety of cells. Three DFRxxL motifs at the kinase N-terminus (residues 2–63) are critical for high-affinity binding to actin-containing filaments [Smith et al. (1999) J. Biol. Chem. 274, 29433–29438]. A GST fusion protein containing residues 1–75 of MLCK (GST75-MLCK) bound maximally to both smooth muscle myofilaments and F-actin at 0.28 and 0.31 mol GST75-MLCK/mol actin with respective K _D values of 0.1 μM and 0.8 μM. High-affinity binding of MLCK to actin-containing filaments may be due to each DFRxxL motif binding to one actin monomer in filaments.

【 授权许可】

Unknown