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J. Biochem, 2003, Vol. 134, No. 3 427-432
© 2003 Japanese Biochemical Society

BIOCHEMISTRY

Structural Elucidation of the Protein- and Membrane-Binding Properties of the N-Terminal Tail Domain of Human Annexin II

Yoon-Hun Hong, Hyung-Sik Won, Hee-Chul Ahn and Bong-Jin Lee*

National Research Laboratory (MPS), College of Pharmacy, Seoul National University, San 56-1, Shillim-Dong, Kwanak-Gu, Seoul 151-742, Korea

The conformational preferences and the solution structure of AnxIIN31, a peptide corresponding to the full-length sequence (residues 1–31) of the human annexin II N-terminal tail domain, were investigated by circular dichroism (CD) and nuclear magnetic resonance (NMR) spectroscopy. CD results showed that AnxIIN31 adopts a mainly {alpha}-helical conformation in hydrophobic or membrane-mimetic environments, while a predominantly random structure is adopted in aqueous buffer. In contrast to previous results of the annexin I N-terminal domain peptide [Yoon et al. (2000) FEBS Lett. 484, 241–245], calcium ions showed no effect on the structure of AnxIIN31. The NMR-derived structure of AnxIIN31 in 50% TFE/water mixture showed a horseshoe-like fold comprising the N-terminal amphipathic {alpha}-helix, the following loop, and the C-terminal helical region. Together, the results establish the first detailed structural data on the N-terminal tail domain of annexin II, and suggest the possibility of the domain to undergo Ca2+-independent membrane-binding.

* To whom correspondence should be addressed. Fax: +82-2-872-3632, E-mail: lbj{at}nmr.snu.ac.kr


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