1CE0

TRIMERIZATION SPECIFICITY IN HIV-1 GP41: ANALYSIS WITH A GCN4 LEUCINE ZIPPER MODEL

1CE0 の概要

• エントリーDOI: 10.2210/pdb1ce0/pdb
• 分子名称: PROTEIN (LEUCINE ZIPPER MODEL H38-P1) (2 entities in total)
• 機能のキーワード: hiv-1 envelope protein, gp41, protein oligomerization, coiled coil, leucine zipper
• 由来する生物種: Human immunodeficiency virus 1
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 13587.87

構造登録者

Shu, W.,Ji, H.,Lu, M. (登録日: 1999-03-12, 公開日: 1999-03-19, 最終更新日: 2023-08-09)

主引用文献

Shu, W.,Ji, H.,Lu, M.
Trimerization specificity in HIV-1 gp41: analysis with a GCN4 leucine zipper model.
Biochemistry, 38:5378-5385, 1999

PubMed 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.

PubMed: 10220324
DOI: 10.1021/bi990199w

実験手法

X-RAY DIFFRACTION (2.4 Å)