Abstract:
:The folding of HIV gp41 into a 6-helix bundle drives virus-cell membrane fusion. To examine the structural relationship between the 6-helix bundle core domain and other regions of gp41, we expressed in Escherichia coli, the entire ectodomain of HIV-2(ST) gp41 as a soluble, trimeric maltose-binding protein (MBP)/gp41 chimera. Limiting proteolysis indicated that the Cys-591-Cys-597 disulfide-bonded region is outside a core domain comprising two peptides, Thr-529-Trp-589 and Val-604-Ser-666. A biochemical examination of MBP/gp41 chimeras encompassing these core peptides indicated that the N-terminal polar segment, 521-528, and C-terminal membrane-proximal segment, 658-666, cooperate in stabilizing the ectodomain. A functional interaction between sequences outside the gp41 core may contribute energy to membrane fusion.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Lay CS,Wilson KA,Kobe B,Kemp BE,Drummer HE,Poumbourios Pdoi
10.1016/j.febslet.2004.04.054keywords:
subject
Has Abstractpub_date
2004-06-04 00:00:00pages
183-8issue
2-3eissn
0014-5793issn
1873-3468pii
S0014579304005332journal_volume
567pub_type
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