Cited by 59T-cell and Retrovirus StudiesProtein Structure and DynamicsHIV Research and Treatment

Three-dimensional structure of the HTLV-II matrix protein and comparative analysis of matrix proteins from the different classes of pathogenic human retroviruses

Christensen, Allyson M., Massiah, Michael A., Turner, Brian G., Sundquist, Wesley I., Summers, Michael F.·1996·Journal of Molecular Biology

Abstract

The matrix protein performs similar roles in all retroviruses, initially directing membrane localization of the assembling viral particle and subsequently forming a stable structural shell associated with the inner surface of the mature viral membrane. Although conserved structural elements are likely to perform these functions in all retroviral matrix proteins, invariant motifs are not evident at the primary sequence level and three-dimensional structures have been available for only the primate lentiviral matrix proteins. We have therefore used NMR spectroscopy to determine the structure of the matrix protein from human T-cell leukemia virus type II (HTLV-II), a member of the human oncovirus subclass of retroviruses. A total of 577 distance restraints were used to build 20 refined models that superimpose with an rmsd of 0.71 A for the backbone atoms of the structured regions. The globular HTLV-II matrix structure is composed of four alpha-helices and a 3(10) helix. Exposed basic residues near the C terminus of helix II form a putative membrane binding surface which could act in concert with the N-terminal myristoyl group to anchor the protein on the viral membrane surface. Clear structural similarities between the HTLV-II and HIV-1 matrix proteins suggest that the topology and exposed cationic membrane binding surface are likely to be conserved features of retroviral matrix proteins.

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Crossref · 10.1006/jmbi.1996.0700

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Authors
Christensen, A. M., Massiah, M. A., Turner, B. G., Sundquist, W. I., & Summers, M. F.
Affiliations
University of Maryland, Baltimore (US)
Corresponding author
Sundquist, Wesley I.
Venue
Journal of Molecular Biology
Publisher
Elsevier BV
Published
1996-12
Volume
264
Issue
5
Pages
1117-1131
ISSN
0022-2836 (ISSN-L)
OpenAlex
W1993573856
Cited by
59
References
11
Citations by year
2025: 2 · 2024: 1 · 2021: 3 · 2020: 1 · 2018: 2 · 2017: 2 · 2016: 1 · 2015: 2 · 2014: 3 · 2013: 3
FWCI
1.71
Type
journal article
Language
en
Open access
closed
Locations
  • Journal of Molecular Biology (publishedVersion)
  • PubMed (publishedVersion)
Funders
National Institute of Allergy and Infectious Diseases (R01AI037524, AI30917)
Topics
  • Life Sciences › Immunology and Microbiology › Immunology › T-cell and Retrovirus Studies
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
  • Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
Keywords
HTLV-II, matrix protein, three-dimensional structure, HIV-1 matrix protein, myristoylation, alpha-helix, 310-helix, structural conservation, viral assembly
MeSH terms
Amino Acid Sequence, Escherichia coli, Humans, Models, Molecular, Molecular Sequence Data, Magnetic Resonance Spectroscopy, Protein Conformation, Recombinant Proteins, Retroviridae, Species Specificity, Viral Matrix Proteins, Human T-lymphotropic virus 2, Human T-lymphotropic virus 1, HIV-1, Sequence Homology, Amino Acid, Protein Structure, Secondary, Protein Structure, Tertiary

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