![]() ![]() Structural basis of Janus kinase trans-activation.The structure of the ternary complex provides a topological blueprint for the orientation and proximity of Frizzled and LRP6 within the Wnt cell surface signalosome. Synthetic peptides comprising the linker domain serve as Wnt-specific antagonists. Chimeric Wnts bearing modular linker "grafts" were able to transfer LRP6 domain specificity between different Wnts and enable non-canonical Wnt5a to signal through the canonical pathway. The cryo-EM structure of a ternary initiation complex of an affinity-matured XWnt8-Frizzled8-LRP6 complex elucidates the basis of coreceptor discrimination by canonical Wnts by means of their N termini and linker domains that engage the LRP6 E1E2 domain funnels. Canonical Wnts form ternary receptor complexes composed of tissue-specific Frizzled (Fzd) receptors together with the shared LRP5/6 coreceptors to initiate β-catenin signaling. Wnt morphogens are critical for embryonic development and tissue regeneration. Undergraduate Research SBIO 199 (Aut, Win, Spr, Sum).Undergraduate Research MCP 199 (Aut, Win, Spr, Sum).Undergraduate Research IMMUNOL 199 (Aut, Win, Spr, Sum).Teaching in Immunology IMMUNOL 290 (Aut, Win, Spr, Sum).Out-of-Department Undergraduate Research BIO 199X (Aut, Win, Spr).Medical Scholars Research SBIO 370 (Aut, Win, Spr, Sum).Medical Scholars Research MCP 370 (Aut, Win, Spr, Sum).Graduate Research SBIO 399 (Aut, Win, Spr, Sum).Graduate Research MCP 399 (Aut, Win, Spr, Sum).Graduate Research IMMUNOL 399 (Aut, Win, Spr, Sum).Graduate Research BIOPHYS 300 (Aut, Win, Spr, Sum).Early Clinical Experience in Immunology IMMUNOL 280 (Aut, Win, Spr, Sum).Directed Reading in Structural Biology SBIO 299 (Aut, Win, Spr, Sum).Directed Reading in Molecular and Cellular Physiology MCP 299 (Aut, Win, Spr, Sum).Directed Reading in Immunology IMMUNOL 299 (Aut, Win, Spr, Sum).Directed Reading in Biophysics BIOPHYS 399 (Aut, Win, Spr, Sum).Directed Investigation BIOE 392 (Aut, Win, Spr, Sum).using combinatorial biology approaches, novel ligands for receptors, which may have altered activities, that may serve as therapeutic starting points. An emerging focus of our research is to develop. Molecules currently under study include receptors of the immune system involved in autoimmune disorders (T cell receptors, co-receptors, MHC, cytokines), proteins involved in host-pathogen interactions and molecular mimicry (CMV and Toxoplasma surface antigens), proteins of nervous system (peptide hormone receptors, neural guidance proteins), and membrane proteins (chemokine receptors). The structural studies are complemented by functional approaches using molecular biology and protein engineering to dissect the structural information, design new or altered proteins with modified specificities and activities, and ultimately contribute to the development of proteins or molecules with therapeutic potential. Many of the systems we are studying in the laboratory are related to the interaction of the host with the environment. Our investigations are aimed at understanding the molecular recognition properties governing the interactions of receptors with their ligands, and the subsequent molecular events which couple ligand recognition to receptor activation. My laboratory studies the structural and functional basis of receptor/ligand interactions in systems which are relevant to human health and disease. Vice Provost for Undergraduate Education.Office of Vice President for Business Affairs and Chief Financial Officer.Office of VP for University Human Resources.Stanford Woods Institute for the Environment.Stanford Institute for Economic Policy Research (SIEPR).Institute for Stem Cell Biology and Regenerative Medicine.Institute for Human-Centered Artificial Intelligence (HAI).Institute for Computational and Mathematical Engineering (ICME).Freeman Spogli Institute for International Studies.Stanford Doerr School of Sustainability. ![]()
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