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.
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Structure (London, England : 1993), 2011, 19 (12), pp.1762-72
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http://hal.univ-grenoble-alpes.fr/hal-01243659
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Soumis le : mardi 15 décembre 2015 - 11:39:16
Dernière modification le : jeudi 11 janvier 2018 - 06:21:39

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Jonathan Elegheert, Ambroise Desfosses, Alexander V Shkumatov, Xiongwu Wu, Nathalie Bracke, et al.. Extracellular complexes of the hematopoietic human and mouse CSF-1 receptor are driven by common assembly principles.. Structure (London, England : 1993), 2011, 19 (12), pp.1762-72. 〈hal-01243659〉

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