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X-ray structures of the hexameric building block of the HIV capsid

Academic Article
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Overview

authors

  • Pornillos, O.
  • Ganser-Pornillos, B. K.
  • Kelly, B. N.
  • Hua, Y. Z.
  • Whitby, F. G.
  • Stout, C. David
  • Sundquist, W. I.
  • Hill, C. P.
  • Yeager, Mark

publication date

  • June 2009

journal

  • Cell  Journal

abstract

  • The mature capsids of HIV and other retroviruses organize and package the viral genome and its associated enzymes for delivery into host cells. The HIV capsid is a fullerene cone: a variably curved, closed shell composed of approximately 250 hexamers and exactly 12 pentamers of the viral CA protein. We devised methods for isolating soluble, assembly-competent CA hexamers and derived four crystallographically independent models that define the structure of this capsid assembly unit at atomic resolution. A ring of six CA N-terminal domains form an apparently rigid core, surrounded by an outer ring of C-terminal domains. Mobility of the outer ring appears to be an underlying mechanism for generating the variably curved lattice in authentic capsids. Hexamer-stabilizing interfaces are highly hydrated, and this property may be key to the formation of quasi-equivalent interactions within hexamers and pentamers. The structures also clarify the molecular basis for capsid assembly inhibition and should facilitate structure-based drug design strategies.

subject areas

  • Capsid Proteins
  • Crystallography, X-Ray
  • HIV-1
  • Models, Molecular
  • Polymers
  • Protein Structure, Tertiary
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Identity

PubMed Central ID

  • PMC2840706

International Standard Serial Number (ISSN)

  • 0092-8674

Digital Object Identifier (DOI)

  • 10.1016/j.cell.2009.04.063

PubMed ID

  • 19523676
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Additional Document Info

start page

  • 1282

end page

  • 1292

volume

  • 137

issue

  • 7

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