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

Jonathan Elegheert UGent, Ambroise Desfosses, Alexander V Shkumatov, Xiongwu Wu, Nathalie Bracke UGent, Kenneth Verstraete UGent, Kathleen Van Craenenbroeck UGent, Bernard R Brooks, Dmitri I Svergun and Bjorn Vergauwen UGent, et al. (2011) STRUCTURE. 19(12). p.1762-1772
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.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
STEM-CELL FACTOR, COLONY-STIMULATING FACTOR, SMALL-ANGLE SCATTERING, RAY SOLUTION SCATTERING, CRYSTAL-STRUCTURE, TYROSINE KINASES, ELECTRON-MICROSCOPY, FLT3 LIGAND, BIOLOGICAL MACROMOLECULES, TRANSMEMBRANE DOMAINS
journal title
STRUCTURE
Structure
volume
19
issue
12
pages
1762 - 1772
Web of Science type
Article
Web of Science id
000297907900010
JCR category
BIOPHYSICS
JCR impact factor
6.347 (2011)
JCR rank
8/71 (2011)
JCR quartile
1 (2011)
ISSN
0969-2126
DOI
10.1016/j.str.2011.10.012
language
English
UGent publication?
yes
classification
A1
copyright statement
I have transferred the copyright for this publication to the publisher
id
2103090
handle
http://hdl.handle.net/1854/LU-2103090
date created
2012-05-09 20:49:46
date last changed
2012-05-10 10:44:36
@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},
  keyword      = {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},
}

Chicago
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.
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.
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.
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.