4bq6

Crystal structure of the RGMB-NEO1 complex form 1

spinqualitylabelsall models 4bq6, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4bq6 is a 6 chain structure with sequence from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.3Å Ligands: NAG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function NEO1_MOUSE May be involved as a regulatory protein in the transition of undifferentiated proliferating cells to their differentiated state. May also function as a cell adhesion molecule in a broad spectrum of embryonic and adult tissues. Publication Abstract from PubMed 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). The RGMB structure reveals a novel protein fold, a functionally important autocatalytic cleavage mechanism and provides a framework to explain numerous disease-linked mutations in RGMs. In the complex, two RGMB ectodomains conformationally stabilize the juxtamembrane regions of two NEO1 receptors, in a pH-dependent manner. We demonstrate that all RGM-NEO1 complexes share this architecture, which therefore represents the core of multiple signaling pathways. Structure of the Repulsive Guidance Molecule (RGM)-Neogenin Signaling Hub.,Bell CH, Healey E, van Erp S, Bishop B, Tang C, Gilbert RJ, Aricescu AR, Pasterkamp RJ, Siebold C Science. 2013 Jun 6. PMID:23744777 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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