title: Dissecting a Hub for Immune Response: Modeling the Structure of MyD88.
abstract: Immune cells sense foreign organisms through the evolutionarily conserved family of Toll-like receptors. Signaling from these receptors relies on oligomerization of adaptor molecules. In this issue of Structure, Vynke et al. (2016) shed light on the dynamical structure of the homo- and hetero-dimerization domain of MyD88, the main adaptor utilized by Toll-like receptors.
authors.affiliation: Department of Biomedicine and Prevention, University of Rome Tor Vergata, 00133 Rome, Italy; Laboratory of Neuroembryology, Fondazione Santa Lucia, 00143 Rome, Italy.
authors.forename: Chiara
authors.initials: C
authors.lastname: Naro
authors.affiliation: Department of Biomedicine and Prevention, University of Rome Tor Vergata, 00133 Rome, Italy; Laboratory of Neuroembryology, Fondazione Santa Lucia, 00143 Rome, Italy. Electronic address: claudio.sette@uniroma2.it.
authors.forename: Claudio
authors.initials: C
authors.lastname: Sette
mesh_terms: D048868:Adaptor Proteins, Signal Transducing / Q000378:metabolism; D006801:Humans; D008562:Membrane Glycoproteins / Q000737:chemistry; D008958:Models, Molecular; D053594:Myeloid Differentiation Factor 88; D011956:Receptors, Cell Surface / Q000737:chemistry; D011971:Receptors, Immunologic / Q000737:chemistry; D017472:Receptors, Interleukin-1; D015398:Signal Transduction; D051193:Toll-Like Receptors / Q000378:metabolism
chemical_list: D048868:Adaptor Proteins, Signal Transducing; D008562:Membrane Glycoproteins; D053594:Myeloid Differentiation Factor 88; D011956:Receptors, Cell Surface; D011971:Receptors, Immunologic; D017472:Receptors, Interleukin-1; D051193:Toll-Like Receptors