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Crystal structure of mouse triggering receptor expressed on myeloid cells 1 (trem-1) at 1.76 Å

Academic Article
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Overview

related to degree

  • Debler, Erik Werner, Ph.D. in Biology, Scripps Research 2002 - 2006
  • Kelker, Matthew, Ph.D. in Biophysics, Scripps Research 2000 - 2005

authors

  • Kelker, Matthew
  • Debler, Erik Werner
  • Wilson, Ian

publication date

  • December 2004

journal

  • Journal of Molecular Biology  Journal

abstract

  • Triggering receptor expressed on myeloid cells (TREM) 1 is an activating receptor expressed on myeloid cells whose ligand(s) remain elusive. TREM-1 stimulation activates neutrophils and monocytes and induces the secretion of pro-inflammatory molecules, which amplifies the Toll-like receptor-initiated responses to invading pathogens. In addition, TREM-1 mediates the septic shock pathway, and thus represents a potential therapeutic target. We report the crystal structure of the mouse TREM-1 extracellular domain at 1.76A resolution. The mouse extracellular domain is monomeric, consistent with our previous human TREM-1 structure, and strongly supports the contention that the globular TREM-1 head is a monomer contrary to proposals of a symmetric dimer.

subject areas

  • Amino Acid Sequence
  • Animals
  • Crystallography, X-Ray
  • Humans
  • Membrane Glycoproteins
  • Mice
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Structure, Tertiary
  • Receptors, Immunologic
  • Sequence Alignment
  • Stereoisomerism
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Research

keywords

  • TREM-1
  • activating receptors
  • crystal structure
  • immune system receptor
  • innate immunity
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Identity

International Standard Serial Number (ISSN)

  • 0022-2836

Digital Object Identifier (DOI)

  • 10.1016/j.jmb.2004.10.009

PubMed ID

  • 15561137
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Additional Document Info

start page

  • 1175

end page

  • 1181

volume

  • 344

issue

  • 5

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