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Title | Extracellular complexes of the hematopoietic human and mouse CSF-1 receptor are driven by common assembly principles. |
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Journal, issue, pages | Structure, Vol. 19, Issue 12, Page 1762-1772, Year 2011 |
Publish date | Dec 7, 2011 |
![]() | Jonathan Elegheert / Ambroise Desfosses / Alexander V Shkumatov / Xiongwu Wu / Nathalie Bracke / Kenneth Verstraete / Kathleen Van Craenenbroeck / Bernard R Brooks / Dmitri I Svergun / Bjorn Vergauwen / Irina Gutsche / Savvas N Savvides / ![]() |
PubMed 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 ...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. |
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Methods | EM (single particle) |
Resolution | 23.0 Å |
Structure data | ![]() EMDB-1977: |
Source |
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