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Protein Science, Vol 6, Issue 7 1583-1586, Copyright © 1997 by Cold Spring Harbor Laboratory Press

FOR THE RECORD

Cloning, purification, and preliminary characterization by circular dichroism and NMR of a carboxyl-terminal domain of the bacteriophage P22 scaffolding protein

M. H. PARKER, M. JABLONSKY, S. CASJENS, L. SAMPSON, N. R. KRISHNA and P. E. PREVELIGE-JR.
Department of Microbiology, University of Alabama at Birmingham, Birmingham, Alabama 35294

Assembly of double-stranded DNA viruses and bacteriophages involves the polymerization of several hundred molecules of coat protein, directed by an internal scaffolding protein. A 163-amino acid carboxyl-terminal fragment of the 303-amino acid bacteriophage P22 scaffolding protein was cloned, overexpressed, and purified. This fragment is active in procapsid assembly reactions in vitro. The circular dichroism spectrum of the fragment, as well as the 1D-NMR and (15)N-(1)H HSQC spectra of the uniformly-labeled protein, indicate that stable secondary structure elements are present. Determination of the three dimensional packing of these elements into the folded scaffolding protein fragment is underway. Structure-based drug design targeted at structural proteins required for viral assembly may have potential as a therapeutic strategy.
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This article has been cited by other articles:


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S. D. Moore and P. E. Prevelige Jr.
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B. Greene and J. King
In Vitro Unfolding/Refolding of Wild Type Phage P22 Scaffolding Protein Reveals Capsid-binding Domain
J. Biol. Chem., June 4, 1999; 274(23): 16135 - 16140.
[Abstract] [Full Text] [PDF]

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B. Greene and J. King
Folding and Stability of Mutant Scaffolding Proteins Defective in P22 Capsid Assembly
J. Biol. Chem., June 4, 1999; 274(23): 16141 - 16146.
[Abstract] [Full Text] [PDF]


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