Three‐dimensional NMR structure of the sixth ligand‐binding module of the human LDL receptor: comparison of two adjacent modules with different ligand binding specificities

FEBS Letters

Kroon, Paulus A.²  Smith, Ross²  Brereton, Ian M.¹  Clayton, Daniel² 

[1] Centre for Magnetic Resonance, University of Queensland, Brisbane, Qld. 4072, Australia;Department of Biochemistry, University of Queensland, Brisbane, Qld. 4072, Australia

关键词: Low-density lipoprotein receptor;    Ligand-binding domain;    Ligand specificity;    Surface property;    Nuclear magnetic resonance spectroscopy;    Three-dimensional structure;    LDLR;    low-density lipoprotein receptor;    LB;    cysteine-rich modules of the ligand-binding domain of LDLR;    TOCSY;    total correlation spectroscopy;    NOESY;    nuclear Overhauser effect spectroscopy;    DQF-COSY;    double-quantum filtered correlation spectroscopy;    E-COSY;    exclusive correlation spectroscopy;    DYANA;    dynamics algorithm for NMR applications;    VDW;    van der Waals;    rmsd;    root mean square deviation;   

DOI  :  10.1016/S0014-5793(00)01842-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The sixth ligand-binding module of the low-density lipoprotein receptor contributes to the binding of apolipoprotein B100-containing lipoproteins. ¹H NMR spectroscopy, DYANA and X-PLOR structure calculations were used to determine that this module has a well defined structure with a backbone conformation similar to other modules. Structures from calculations that simulated the presence of a calcium ion showed increased resolution without large increases in energy, increased deviations from idealised geometry or violations of experimental constraints. Investigation of the surface properties of this module indicates there are significant differences from the fifth module, which binds apolipoprotein E-containing lipoproteins in addition to apolipoprotein B100-containing lipoproteins.

【 授权许可】

Unknown