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April 15, 1993The Journal of Cell BiologyOpen Access

A novel integrin specificity exemplified by binding of the alpha v beta 5 integrin to the basic domain of the HIV Tat protein and vitronectin.

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Authors

BVBjörn VogelNational Foundation for Cancer ResearchSLS J LeeKorea Research Institute of Bioscience and BiotechnologyAHA. HildebrandOtto-von-Guericke University Magdeburg

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Implication

Randomized trial uncovers novel integrin binding in HIV Tat protein, indicating significant interaction implications.

Key Points

  • This research investigates the binding specificity of the alpha v beta 5 integrin to the basic domain of the HIV Tat protein and vitronectin.
  • Analyzed cell attachment activity of Tat and derived peptides.
  • Utilized affinity chromatography for assessing integrin binding with Tat peptides.
  • Conducted immunoprecipitation with anti-integrin antibodies to identify binding partners.
  • Alpha v beta 5 integrin binds to the basic domain of Tat (RKKRRQRRR), showing an atypical binding mechanism.
  • The related vitronectin sequence (KKQRFRHRNRKG) also binds to alpha v beta 5 and can inhibit cell attachment.
  • Binding of alpha v beta 5 to Tat is divalent cation independent, differing from its binding to RGD-containing peptides.

Cite This Study

Vogel et al. (1993) studied this question.

synapsesocial.com/papers/6a64fcb7fac10bc8e2c6d577https://doi.org/10.1083/jcb.121.2.461
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Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Receptor functions for the integrin VLA-3: fibronectin, collagen, and laminin binding are differentially influenced by Arg-Gly-Asp peptide and by divalent cations.1991 · 448 citations
  2. 2Characterization of the integrin alpha v beta 6 as a fibronectin-binding protein.1992 · 293 citations
  3. 3Trans -Activator Gene of Human T-Lymphotropic Virus Type III (HTLV-III)1985 · 864 citations
  4. 4New Perspectives in Cell Adhesion: RGD and Integrins1987 · 4,905 citations
  5. 5Biosynthetic and functional properties of an Arg-Gly-Asp-directed receptor involved in human melanoma cell attachment to vitronectin, fibrinogen, and von Willebrand factor.1987 · 571 citations