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Instruments / Technical Area	Publication Details	Published	Actions
I03-Macromolecular Crystallography I04-1-Macromolecular Crystallography (fixed wavelength) I04-Macromolecular Crystallography	Repulsive guidance molecule is a structural bridge between neogenin and bone morphogenetic protein Eleanor Healey , Benjamin Bishop , Jonathan Elegheert , Christian Bell , Sergi Padilla-parra , Christian Siebold Nature Structural & Molecular Biology 22 (6), 458 - 465 DOI: 10.1038/nsmb.3016 PMID: 25938661 Diamond Proposal Number(s): [10627] Open Access Show Abstract ▼ Abstract: Repulsive guidance molecules (RGMs) control crucial processes including cell motility, adhesion, immune-cell regulation and systemic iron metabolism. RGMs signal via the neogenin (NEO1) and the bone morphogenetic protein (BMP) pathways. Here, we report crystal structures of the N-terminal domains of all human RGM family members in complex with the BMP ligand BMP2, revealing a new protein fold and a conserved BMP-binding mode. Our structural and functional data suggest a pH-linked mechanism for RGM-activated BMP signaling and offer a rationale for RGM mutations causing juvenile hemochromatosis. We also determined the crystal structure of the ternary BMP2–RGM–NEO1 complex, which, along with solution scattering and live- cell super-resolution fluorescence microscopy, indicates BMP-induced clustering of the RGM–NEO1 complex. Our results show how RGM acts as the central hub that links BMP and NEO1 and physically connects these fundamental signaling pathways.	May 2015
I03-Macromolecular Crystallography	Structure of the Repulsive Guidance Molecule (RGM)-Neogenin Signaling Hub Christian H. Bell , Eleanor Healey , Susan Van Erp , Benjamin Bishop , Chenxiang Tang , Robert J. C. Gilbert , Alexandru Aricescu , R. Jeroen Pasterkamp , Christian Siebold Science 341 (6141), 77 - 80 DOI: 10.1126/science.1232322 PMID: 23744777 Diamond Proposal Number(s): [8423] Show Abstract ▼ Abstract: Repulsive guidance molecule family members (RGMs) control fundamental and diverse cellular processes, including motility and adhesion, immune cell regulation, and systemic iron metabolism. However, it is not known how RGMs initiate signaling through their common cell-surface receptor, neogenin (NEO1). Here, we present crystal structures of the NEO1 RGM-binding region and its complex with human RGMB (also called dragon).	Jul 2013

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