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Extracellular complexes of the hematopoietic human and mouse CSF-1 receptor are driven by common assembly principles

(2011) STRUCTURE. 19(12). p.1762-1772
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Abstract
The hematopoietic colony stimulating factor-1 receptor (CSF-1R or FMS) is essential for the cellular repertoire of the mammalian immune system. Here, we report a structural and mechanistic consensus for the assembly of human and mouse CSF-1 :CSF-1R complexes. The EM structure of the complete extracellular assembly of the human CSF-1:CSF-1R complex reveals how receptor dimerization by CSF-1 invokes a ternary complex featuring extensive homotypic receptor contacts and striking structural plasticity at the extremities of the complex. Studies by small-angle X-ray scattering of unliganded hCSF-1R point to large domain rearrangements upon CSF-1 binding, and provide structural evidence for the relevance of receptor predimerization at the cell surface. Comparative structural and binding studies aiming to dissect the assembly principles of human and mouse CSF-1R complexes, including a quantification of the CSF-1/CSF-1R species cross-reactivity, show that bivalent cytokine binding to receptor coupled to ensuing receptor-receptor interactions are common denominators in extracellular complex formation.
Keywords
STEM-CELL FACTOR, COLONY-STIMULATING FACTOR, SMALL-ANGLE SCATTERING, RAY SOLUTION SCATTERING, CRYSTAL-STRUCTURE, TYROSINE KINASES, ELECTRON-MICROSCOPY, FLT3 LIGAND, BIOLOGICAL MACROMOLECULES, TRANSMEMBRANE DOMAINS

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MLA
Elegheert, Jonathan, Ambroise Desfosses, Alexander V Shkumatov, et al. “Extracellular Complexes of the Hematopoietic Human and Mouse CSF-1 Receptor Are Driven by Common Assembly Principles.” STRUCTURE 19.12 (2011): 1762–1772. Print.
APA
Elegheert, J., Desfosses, A., Shkumatov, A. V., Wu, X., Bracke, N., Verstraete, K., Van Craenenbroeck, K., et al. (2011). Extracellular complexes of the hematopoietic human and mouse CSF-1 receptor are driven by common assembly principles. STRUCTURE, 19(12), 1762–1772.
Chicago author-date
Elegheert, Jonathan, Ambroise Desfosses, Alexander V Shkumatov, Xiongwu Wu, Nathalie Bracke, Kenneth Verstraete, Kathleen Van Craenenbroeck, et al. 2011. “Extracellular Complexes of the Hematopoietic Human and Mouse CSF-1 Receptor Are Driven by Common Assembly Principles.” Structure 19 (12): 1762–1772.
Chicago author-date (all authors)
Elegheert, Jonathan, Ambroise Desfosses, Alexander V Shkumatov, Xiongwu Wu, Nathalie Bracke, Kenneth Verstraete, Kathleen Van Craenenbroeck, Bernard R Brooks, Dmitri I Svergun, Bjorn Vergauwen, Irina Gutsche, and Savvas Savvides. 2011. “Extracellular Complexes of the Hematopoietic Human and Mouse CSF-1 Receptor Are Driven by Common Assembly Principles.” Structure 19 (12): 1762–1772.
Vancouver
1.
Elegheert J, Desfosses A, Shkumatov AV, Wu X, Bracke N, Verstraete K, et al. Extracellular complexes of the hematopoietic human and mouse CSF-1 receptor are driven by common assembly principles. STRUCTURE. 2011;19(12):1762–72.
IEEE
[1]
J. Elegheert et al., “Extracellular complexes of the hematopoietic human and mouse CSF-1 receptor are driven by common assembly principles,” STRUCTURE, vol. 19, no. 12, pp. 1762–1772, 2011.
@article{2103090,
  abstract     = {{The hematopoietic colony stimulating factor-1 receptor (CSF-1R or FMS) is essential for the cellular repertoire of the mammalian immune system. Here, we report a structural and mechanistic consensus for the assembly of human and mouse CSF-1 :CSF-1R complexes. The EM structure of the complete extracellular assembly of the human CSF-1:CSF-1R complex reveals how receptor dimerization by CSF-1 invokes a ternary complex featuring extensive homotypic receptor contacts and striking structural plasticity at the extremities of the complex. Studies by small-angle X-ray scattering of unliganded hCSF-1R point to large domain rearrangements upon CSF-1 binding, and provide structural evidence for the relevance of receptor predimerization at the cell surface. Comparative structural and binding studies aiming to dissect the assembly principles of human and mouse CSF-1R complexes, including a quantification of the CSF-1/CSF-1R species cross-reactivity, show that bivalent cytokine binding to receptor coupled to ensuing receptor-receptor interactions are common denominators in extracellular complex formation.}},
  author       = {{Elegheert, Jonathan and Desfosses, Ambroise and Shkumatov, Alexander V and Wu, Xiongwu and Bracke, Nathalie and Verstraete, Kenneth and Van Craenenbroeck, Kathleen and Brooks, Bernard R and Svergun, Dmitri I and Vergauwen, Bjorn and Gutsche, Irina and Savvides, Savvas}},
  issn         = {{0969-2126}},
  journal      = {{STRUCTURE}},
  keywords     = {{STEM-CELL FACTOR,COLONY-STIMULATING FACTOR,SMALL-ANGLE SCATTERING,RAY SOLUTION SCATTERING,CRYSTAL-STRUCTURE,TYROSINE KINASES,ELECTRON-MICROSCOPY,FLT3 LIGAND,BIOLOGICAL MACROMOLECULES,TRANSMEMBRANE DOMAINS}},
  language     = {{eng}},
  number       = {{12}},
  pages        = {{1762--1772}},
  title        = {{Extracellular complexes of the hematopoietic human and mouse CSF-1 receptor are driven by common assembly principles}},
  url          = {{http://dx.doi.org/10.1016/j.str.2011.10.012}},
  volume       = {{19}},
  year         = {{2011}},
}

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