Structure of the Active Domain of the Herpes Simplex Virus Protein ICP47 in Water/Sodium Dodecyl Sulfate Solution Determined by Nuclear Magnetic Resonance Spectroscopy
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- 作者：Ruth Pfä ; nder ; Lars Neumann ; Markus Zweckstetter ; Christoph Seger ; Tad A. Holak ; and Robert Tampé
- 刊名：Biochemistry
- 出版年：1999
- 出版时间：October 12, 1999
- 年：1999
- 卷：38
- 期：41
- 页码：13692 - 13698
- 全文大小：144K
- 年卷期：v.38,no.41(October 12, 1999)
- ISSN：1520-4995
文摘
ICP47 encoded by herpes simplex virus (HSV) is a key factor in the evasion of cellular immuneresponse against HSV-infected cells. By specific inhibition of the transporter associated with antigenprocessing (TAP), ICP47 prevents peptide transport into the endoplasmic reticulum and subsequent loadingof major histocompatibility complex (MHC) class I molecules. Amino acid residues 3-34 have beenidentified as the active domain. This domain appeared to be unstructured in aqueous solution, whereasafter binding to membranes an 
-helical conformation was observed. Here, we have analyzed the structureof ICP47(2-34) in a lipidlike environment by nuclear magnetic resonance (NMR) spectroscopy. In micellarsolution of deuterated sodium dodecyl sulfate, the viral TAP inhibitor adopts an ordered structure. Thereare two helical regions extending from residues 4 to 15 and from residues 22 to 32. Arg-16 is found onthe C-terminus of the first helix, and Gly-33 serves as a terminator of the second helix. A loop betweenresidues 17 and 21 is also evident in the structure. The relative orientation of the helices toward eachother, however, could not be determined due to the paucity of NOEs from residues 18-21.
-helical conformation was observed. Here, we have analyzed the structureof ICP47(2-34) in a lipidlike environment by nuclear magnetic resonance (NMR) spectroscopy. In micellarsolution of deuterated sodium dodecyl sulfate, the viral TAP inhibitor adopts an ordered structure. Thereare two helical regions extending from residues 4 to 15 and from residues 22 to 32. Arg-16 is found onthe C-terminus of the first helix, and Gly-33 serves as a terminator of the second helix. A loop betweenresidues 17 and 21 is also evident in the structure. The relative orientation of the helices toward eachother, however, could not be determined due to the paucity of NOEs from residues 18-21.