Cited by 5HIV Research and TreatmentProtein Structure and DynamicsEnzyme Structure and Function

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Domain Organization of Lentiviral and Betaretroviral Surface Envelope Glycoproteins Modeled with AlphaFold

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Hötzel, Isidro·2022·Journal of Virology

Published version of a preprint

Abstract

Structural information on the surface envelope proteins of lentiviruses and related betaretroviruses is critical to understand mechanisms of virus-host interactions. However, experimental determination of these structures has been challenging, and only the structure of the human immunodeficiency virus type 1 gp120 has been determined.

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Metadata

Authors
Hötzel, I.
Affiliations
Genentech (US)
Corresponding author
Hötzel, Isidro
Venue
Journal of Virology
Published
2022-01-26
Volume
96
Issue
2
Pages
e0134821-e0134821
ISSN
  • 0022-538X (ISSN-L)
  • 1098-5514
OpenAlex
W3210736751
Cited by
5
References
3
Citations by year
2025: 1 · 2024: 1 · 2023: 2 · 2022: 1
FWCI
0.56
Type
journal article
Language
en
Open access
Locations
  • Journal of Virology (publishedVersion)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
Keywords
small ruminant lentivirus, AlphaFold structure prediction, domain organization, host-virus interaction, receptor binding domain, immune evasion, viral entry mechanism
MeSH terms
Protein Domains, Algorithms, Amino Acid Sequence, Animals, Binding Sites, Humans, Models, Molecular, Protein Binding, Receptors, Virus, Ruminants, Gene Products, env, Lentivirus, Conserved Sequence, Endogenous Retroviruses, Betaretrovirus

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