"DTIC ADA429781: The Anthrax Protective Antigen (PA63) Bound Conformation Of A Peptide Inhibitor Of The Binding Of Lethal Factor To PA63: As Determined By TrNOESY NMR And Molecular Modelling" - Information and Links:

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"DTIC ADA429781: The Anthrax Protective Antigen (PA63) Bound Conformation Of A Peptide Inhibitor Of The Binding Of Lethal Factor To PA63: As Determined By TrNOESY NMR And Molecular Modelling" and the language of the book is English.


“DTIC ADA429781: The Anthrax Protective Antigen (PA63) Bound Conformation Of A Peptide Inhibitor Of The Binding Of Lethal Factor To PA63: As Determined By TrNOESY NMR And Molecular Modelling” Metadata:

  • Title: ➤  DTIC ADA429781: The Anthrax Protective Antigen (PA63) Bound Conformation Of A Peptide Inhibitor Of The Binding Of Lethal Factor To PA63: As Determined By TrNOESY NMR And Molecular Modelling
  • Author: ➤  
  • Language: English

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  • Internet Archive ID: DTIC_ADA429781

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"DTIC ADA429781: The Anthrax Protective Antigen (PA63) Bound Conformation Of A Peptide Inhibitor Of The Binding Of Lethal Factor To PA63: As Determined By TrNOESY NMR And Molecular Modelling" Description:

The Internet Archive:

Anthrax protective antigen (PA) is one of the three proteins produced by the gram positive bacteria Bacillus anthracis collectively known as the anthrax toxin. The role played by PA in anthrax intoxication is to transport the two enzymes lethal factor (LF) and edema factor (EF) into the cell. Collier and co-workers reported the isolation of two peptides via phage display that bind to the PA63 heptamer and inhibit its interaction with LF and EF, and thereby prevent the transport of LF and EF into the cell. One of these peptides was selected for structural investigation on the basis of its ability to prevent the binding of LF to the PA63 heptamer bundle. Two dimensional trNOESY experiments coupled with NOE restrained simulated annealing calculations were used to determine the PA63-bound conformation of P1. On binding to PA63, P1 adopts a helical conformation involving residues 3-9 while the C- and N-terminal residues exhibit dynamic fraying.

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