solution structure of lc4 transmembrane segment of ccr5解决方案lc4跨膜段ccr5的结构.pdfVIP

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