solution structure of lc4 transmembrane segment of ccr5解决方案lc4跨膜段ccr5的结构.pdf
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Solution Structure of LC4 Transmembrane Segment of
CCR5
1 2
Kazuhide Miyamoto *, Kayo Togiya
1 Department of Pharmaceutical Health Care, Faculty of Pharmaceutical Sciences, Himeji Dokkyo University, Himeji, Hyogo, Japan, 2 15-203 Hirano-machi, Himeji, Hyogo,
Japan
Abstract
CC-chemokine receptor 5 (CCR5) is a specific co-receptor allowing the entry of human immunodeficiency virus type 1 (HIV-1).
The LC4 region in CCR5 is required for HIV-1 entry into the cells. In this study, the solution structure of LC4 in SDS micelles
was elucidated by using standard 1H two-dimensional NMR spectroscopy, circular dichroism, and fluorescdence
quenching. The LC4 structure adopts two helical structures, whereas the C-terminal part remains unstructured. The
positions in which LC4 binds to the HIV-1 inhibitory peptide LC5 were determined by docking calculations in addition to
NMR data. The poses showed the importance of the hydrophobic interface of the assembled structures. The solution
structure of LC4 elucidated in the present work provides a structural basis for further studies on the HIV-1 inhibitory
function of the LC4 region.
Citation: Miyamoto K, Togiya K (2011) Solution Structure of LC4 Transmembrane Segment of CCR5. PLoS ONE 6(5): e20452. doi:10.1371/journal.pone.0020452
Editor: John J. Rossi, Beckman Research Institute of the City of Hope, United States of America
Received February 27, 2011; Accepted April 26, 2011; Published May 27, 2011
Copyright: 2011 Miyamoto, Togiya. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits
unrestricted use, distribution, and reproduction in an
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