1CE0

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


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.40 Å
  • R-Value Free: 0.294 
  • R-Value Work: 0.221 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

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

Shu, W.Ji, H.Lu, M.

(1999) Biochemistry 38: 5378-5385

  • DOI: https://doi.org/10.1021/bi990199w
  • Primary Citation of Related Structures:  
    1CE0

  • 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.


  • Organizational Affiliation

    Department of Biochemistry, Weill Medical College of Cornell University, New York 10021, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
PROTEIN (LEUCINE ZIPPER MODEL H38-P1)
A, B, C
37Human immunodeficiency virus 1Mutation(s): 0 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.40 Å
  • R-Value Free: 0.294 
  • R-Value Work: 0.221 
  • Space Group: P 61
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 50.785α = 90
b = 50.785β = 90
c = 119.251γ = 120
Software Package:
Software NamePurpose
AMoREphasing
X-PLORrefinement
DENZOdata reduction
SCALEPACKdata scaling

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1999-03-19
    Type: Initial release
  • Version 1.1: 2008-04-26
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2019-11-06
    Changes: Data collection, Database references
  • Version 1.4: 2023-08-09
    Changes: Data collection, Database references, Refinement description