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Three-dimensional model of the human platelet integrin alpha(llb)beta(3) based on electron cryomicroscopy and x-ray crystallography

Academic Article
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Overview

authors

  • Adair, B. D.
  • Yeager, Mark

publication date

  • October 2002

journal

  • Proceedings of the National Academy of Sciences of the United States of America  Journal

abstract

  • Integrins are a large family of heterodimeric transmembrane signaling proteins that affect diverse biological processes such as development, angiogenesis, wound healing, neoplastic transformation, and thrombosis. We report here the three-dimensional structure at 20-A resolution of the unliganded, low-affinity state of the human platelet integrin alpha(IIb)beta(3) derived by electron cryomicroscopy and single particle image reconstruction. The large ectodomain and small cytoplasmic domains are connected by a rod of density that we interpret as two parallel transmembrane alpha-helices. The docking of the x-ray structure of the alpha(V)beta(3) ectodomain into the electron cryomicroscopy map of alpha(IIb)beta(3) requires hinge movements at linker regions between domains in the crystal structure. Comparison of the putative high- and low-affinity conformations reveals dramatic conformational changes associated with integrin activation.

subject areas

  • Amino Acid Sequence
  • Binding Sites
  • Cell Membrane
  • Cryoelectron Microscopy
  • Crystallography, X-Ray
  • Cytoplasm
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Platelet Glycoprotein GPIIb-IIIa Complex
  • Protein Structure, Tertiary
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Research

keywords

  • cell adhesion
  • membrane proteins
  • platelets
  • transmembrane signaling
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Identity

PubMed Central ID

  • PMC137836

International Standard Serial Number (ISSN)

  • 0027-8424

Digital Object Identifier (DOI)

  • 10.1073/pnas.212498199

PubMed ID

  • 12388784
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Additional Document Info

start page

  • 14059

end page

  • 14064

volume

  • 99

issue

  • 22

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