Solution structure and membrane‐binding property of the N‐terminal tail domain of human annexin I

FEBS Letters

Park, Sang-Ho²  Lee, Bong-Jin²  Na, Doe-Sun¹  Won, Hyung-Sik²  Yoon, Mi-Kyung² 

[1] Department of Biochemistry, College of Medicine, University of Ulsan, Seoul 138-736, South Korea;College of Pharmacy, Seoul National University, Seoul 151-742, South Korea

关键词: AnxIN26;    Human annexin I;    Nuclear magnetic resonance;    Circular dichroism;    Membrane binding;    AnxIN26;    a peptide corresponding to residues 2 to 26 of human annexin I;    CD;    circular dichroism;    DQF-COSY;    double quantum filtered correlation spectroscopy;    NMR;    nuclear magnetic resonance;    NOE;    nuclear Overhauser effect;    NOESY;    NOE spectroscopy;    r.m.s.d.;    root mean square deviation;    SDS;    sodium dodecyl sulfate;    TFE;    2;    2;    2-trifluoroethanol;    TOCSY;    total correlation spectroscopy;   

DOI  :  10.1016/S0014-5793(00)02160-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The conformational preferences of AnxI^N26, a peptide corresponding to residues 2–26 of human annexin I, were investigated using CD and NMR spectroscopy. CD results showed that AnxI^N26 adopts a mainly α-helical conformation in membrane-mimetic environments, TFE/water and SDS micelles, while a predominantly random structure with slight helical propensity in aqueous buffer. The helical region of AnxI^N26 showed a nearly identical conformation between in TFE/water and in SDS micelles, except for the orientation of the Trp-12 side-chain, which was quite different between the two. The N-terminal region of the AnxI^N26 helix showed a typical amphipathic nature, which could be stabilized by the neighboring hydrophobic cluster. The helical stability of the peptide in SDS micelles was increased by addition of calcium ions. These results suggest that the N-terminal tail domain of human annexin I interacts with biological membranes in a partially calcium-dependent manner.

【 授权许可】

Unknown