Infection by HIV-1 involves the fusion of viral and cellular membranes with subsequent transfer of viral genetic material into the cell.
The HIV-1 envelope glycoprotein that mediates fusion consists of the surface subunit gp120 and the transmembrane subunit gp41.
gp120 directs virion attachment to the cell-surface receptors, and gp41 then promotes viral-cell membrane fusion.
A soluble, alpha-helical, trimeric complex within gp41 composed of N-terminal and C-terminal extraviral segments has been proposed to represent the core of the fusion-active conformation of the HIV-1 envelope.
Three N-terminal helices within the bundle form a central, parallel, trimeric coiled coil, whereas three C-terminal helices pack in the reverse direction into three hydrophobic grooves on the surface of the N-terminal trimer.
This thermostable subdomain displays the salient features of the core structure of the isolated gp41 subunit and thus provides a possible target for therapeutics designed selectively to block HIV-1 entry.
特徴
This protein carries a polyhistidine tag at the C-terminus.
The protein has a calculated MW of 44.3 kDa.
The protein migrates as Band dispersion when calibrated against Star Ribbon Pre-stained Protein Marker under reducing (R) condition (SDS-PAGE).
仕様
容量：50ug
Source：HIV-1 (HXB2) GP41 Pre-hairpin intermediate Protein, His Tag (GP1-H51H3) is expressed from E. coli cells. It contains AA Ala 533 - Leu 856 (Accession # P04578).
