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• W2130455364 abstract "The solution structure of the ectodomain of simian immunodeficiency virus (SIV) gp41 (e-gp41), consisting of residues 27-149, has been determined by multidimensional heteronuclear NMR spectroscopy. SIV e-gp41 is a symmetric 44 kDa trimer with each subunit consisting of antiparallel N-terminal (residues 30-80) and C-terminal (residues 107-147) helices connected by a 26 residue loop (residues 81-106). The N-terminal helices of each subunit form a parallel coiled-coil structure in the interior of the complex which is surrounded by the C-terminal helices located on the exterior of the complex. The loop region is ordered and displays numerous intermolecular and non-sequential intramolecular contacts. The helical core of SIV e-gp41 is similar to recent X-ray structures of truncated constructs of the helical core of HIV-1 e-gp41. The present structure establishes unambiguously the connectivity of the N- and C-terminal helices in the trimer, and characterizes the conformation of the intervening loop, which has been implicated by mutagenesis and antibody epitope mapping to play a key role in gp120 association. In conjunction with previous studies, the solution structure of the SIV e-gp41 ectodomain provides insight into the binding site of gp120 and the mechanism of cell fusion. The present structure of SIV e-gp41 represents one of the largest protein structures determined by NMR to date." @default.
• W2130455364 created "2016-06-24" @default.
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• W2130455364 date "1998-08-17" @default.
• W2130455364 modified "2023-10-18" @default.
• W2130455364 title "Three-dimensional solution structure of the 44kDa ectodomain of SIV gp41" @default.
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• W2130455364 doi "https://doi.org/10.1093/emboj/17.16.4572" @default.
• W2130455364 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1170787" @default.
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• W2130455364 hasPublicationYear "1998" @default.
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