| First Author | Elegheert J | Year | 2011 |
| Journal | Structure | Volume | 19 |
| Issue | 12 | Pages | 1762-72 |
| PubMed ID | 22153499 | Mgi Jnum | J:245355 |
| Mgi Id | MGI:5918492 | Doi | 10.1016/j.str.2011.10.012 |
| Citation | Elegheert J, et al. (2011) Extracellular complexes of the hematopoietic human and mouse CSF-1 receptor are driven by common assembly principles. Structure 19(12):1762-72 |
| abstractText | 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. |
