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Trimerization specificity in HIV-1 gp41: analysis with a GCN4 leucine zipper model.

Shu W, Ji H, Lu M
Biochemistry 38 5378-85 (1999)
Related entries: 1szt, 2zta

Cited: 37 times
EuropePMC logo PMID: 10220324

Abstract

The envelope glycoprotein of human immunodeficiency virus type 1 (HIV-1) consists of a complex of two noncovalently associated subunits, gp120 and gp41. Formation of gp120/gp41 oligomers is thought to be dependent on a 4-3 hydrophobic (heptad) repeat located in the amino-terminal region of the gp41 molecule. We have investigated the role of this heptad repeat in determining the oligomeric structure of gp41 by introducing its buried core residues into the first (a) and fourth (d) positions of the GCN4 leucine-zipper dimerization domain. The mutant peptides fold into trimeric, helical structures, as shown by circular dichroism and equilibrium sedimentation centrifugation. The 2.4 A resolution crystal structure of one such trimer reveals a parallel three-stranded, alpha-helical coiled coil. Thus, the buried core residues from the gp41 heptad repeat direct trimer formation. We suggest that the conserved amino-terminal heptad repeat within the gp41 ectodomain possesses trimerization specificity.

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Related citations provided by authors (2)

  1. X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil.. O'Shea EK, Klemm JD, Kim PS, Alber T Science 254 539-44 (1991)
  2. Atomic structure of a thermostable subdomain of HIV-1 gp41.. Tan K, Liu J, Wang J, Shen S, Lu M Proc Natl Acad Sci U S A 94 12303-8 (1997)

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