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


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.

SUBMITTER: Elegheert J 

PROVIDER: S-EPMC3260422 | biostudies-literature | 2011 Dec

REPOSITORIES: biostudies-literature

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

Elegheert Jonathan J   Desfosses Ambroise A   Shkumatov Alexander V AV   Wu Xiongwu X   Bracke Nathalie N   Verstraete Kenneth K   Van Craenenbroeck Kathleen K   Brooks Bernard R BR   Svergun Dmitri I DI   Vergauwen Bjorn B   Gutsche Irina I   Savvides Savvas N SN  

Structure (London, England : 1993) 20111201 12


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  ...[more]

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