低密度脂蛋白受体的结构特征有助于配体的结合与释放。

Structural features of the low-density lipoprotein receptor facilitating ligand binding and release.

作者信息

Beglova N, Jeon H, Fisher C, Blacklow S C

机构信息

Department of Pathology, Brigham and Women's Hospital and Harvard Medical School, 77 Avenue Louis Pasteur, Boston, MA 02115, USA.

出版信息

Biochem Soc Trans. 2004 Nov;32(Pt 5):721-3. doi: 10.1042/BST0320721.

DOI:10.1042/BST0320721

PMID:15493997

Abstract

The LDLR (low-density lipoprotein receptor) is a modular protein built from several distinct structural units: LA (LDLR type-A), epidermal growth factor-like and beta-propeller modules. The low pH X-ray structure of the LDLR revealed long-range intramolecular contacts between the propeller domain and the central LA repeats of the ligand-binding domain, suggesting that the receptor changes its overall shape from extended to closed, in response to pH. Here we discuss how the LDLR uses flexibility and rigidity of linkers between modules to facilitate ligand binding and low-pH ligand release.

摘要

低密度脂蛋白受体（LDLR）是一种由几个不同结构单元构建而成的模块化蛋白质：A型低密度脂蛋白受体（LA）、表皮生长因子样模块和β-螺旋桨模块。LDLR的低pH值X射线结构揭示了螺旋桨结构域与配体结合结构域的中央LA重复序列之间的长程分子内接触，这表明受体响应pH值变化，其整体形状从伸展状态转变为闭合状态。在此，我们讨论LDLR如何利用模块间连接子的灵活性和刚性来促进配体结合以及在低pH值下释放配体。