Contribution of disulfide bonds in the carboxyl terminus of the human immunodeficiency virus type I gp120 glycoprotein to CD4 binding.

Article

Contribution of disulfide bonds in the carboxyl terminus of the human immunodeficiency virus type I gp120 glycoprotein to CD4 binding.

Journal of acquired immune deficiency syndromes - 1 Jan 1992

Lekutis C, Olshevsky U, Furman C, Thali M, Sodroski J

Abstract excerpt

The carboxyl half of the HIV-1 gp120 glycoprotein, which has been implicated in binding to the CD4 receptor, contains two disulfide bonds linking cysteine residues 378-445 and 385-418. To examine the necessity of these disulfide bonds for the formation and/or maintenance of a gp120 glycoprotein c...

Topics

CD4 Antigens
Cell Line
HIV Envelope Protein gp120
HIV-1
Humans
Mutation
Plasmids
Transfection

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