2EZO
SOLUTION NMR STRUCTURE OF ECTODOMAIN OF SIV GP41, RESTRAINED REGULARIZED MEAN STRUCTURE
2EZO の概要
エントリーDOI | 10.2210/pdb2ezo/pdb |
分子名称 | GP41 (1 entity in total) |
機能のキーワード | virus envelope protein, siv gp41 ectodomain, viral protein |
由来する生物種 | Simian immunodeficiency virus |
タンパク質・核酸の鎖数 | 3 |
化学式量合計 | 43293.80 |
構造登録者 | |
主引用文献 | Caffrey, M.,Cai, M.,Kaufman, J.,Stahl, S.J.,Wingfield, P.T.,Covell, D.G.,Gronenborn, A.M.,Clore, G.M. Three-dimensional solution structure of the 44 kDa ectodomain of SIV gp41. EMBO J., 17:4572-4584, 1998 Cited by PubMed 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. PubMed: 9707417DOI: 10.1093/emboj/17.16.4572 主引用文献が同じPDBエントリー |
実験手法 | SOLUTION NMR |
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