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Articles by Ignacio Moraga
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Structural insights into IL-11-mediated signalling and human IL6ST variant-associated immunodeficiency - Nature Communications
Abstract IL-11 and IL-6 activate signalling via assembly of the cell surface receptor gp130; however, it is unclear how signals are transmitted across the membrane to instruct cellular responses. Here we solve the cryoEM structure of the IL-11 receptor recognition complex to discover how differences in gp130-binding interfaces may drive signalling outcomes.
Molecular and cellular factors determining the functional pleiotropy of cytokines
Cytokine-receptor complex geometry and signalling responses While the stability of the cytokine-receptor complex plays a central role in defining cytokine responses, other receptor binding parameters also contribute to fine-tuning cytokine signalling and responses [[132]]. Cytokines bind their receptors in a diverse range of molecular architectures and stoichiometries [[56, 61, 94, 116, 133-141]].
A strategy for the selection of monovalent antibodies that span protein dimer interfaces
Jamie B. Spangler1*, Ignacio Moraga1, Kevin M Jude1, Christina S Savvides2 and K.
A strategy for the selection of monovalent antibodies that span protein dimer interfaces
A strategy for the selection of monovalent antibodies that span protein dimer interfaces
Ligand-induced type II interleukin-4 receptor dimers are sustained by rapid re-association within plasma membrane microcompartments
We characterized the molecular features of the type II IL-4 receptor assembly under well-defined conditions in vitro using a model system based on solid-supported membranes (SSMs)35. For this purpose, the ectodomains of IL-4R? and IL-13R?1 fused to a C-terminal decahistidine tag (IL-4R??EC and IL-13R?1-EC, respectively) were tethered onto SSMs by means of a lipid analogue functionalized with tris-NTA36.
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