4BQ9

Crystal structure of the FN5 and FN6 domains of NEO1, form 1

Summary for 4BQ9

• Entry DOI: 10.2210/pdb4bq9/pdb
• Related: 4BQ6 4BQ7 4BQ8 4BQB 4BQC
• Descriptor: NEOGENIN, 2-acetamido-2-deoxy-beta-D-glucopyranose (2 entities in total)
• Functional Keywords: cell adhesion
• Biological source: MUS MUSCULUS (MOUSE)
• Total number of polymer chains: 2
• Total formula weight: 48595.03

Authors

Bell, C.H.,Healey, E.,van Erp, S.,Bishop, B.,Tang, C.,Gilbert, R.J.C.,Aricescu, A.R.,Pasterkamp, R.J.,Siebold, C. (deposition date: 2013-05-30, release date: 2013-06-12, Last modification date: 2024-11-13)

Primary citation

Bell, C.H.,Healey, E.,Van Erp, S.,Bishop, B.,Tang, C.,Gilbert, R.J.C.,Aricescu, A.R.,Pasterkamp, R.J.,Siebold, C.
Structure of the Repulsive Guidance Molecule (Rgm)-Neogenin Signaling Hub
Science, 341:77-, 2013

PubMed 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). The RGMB structure reveals a previously unknown protein fold and 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.

PubMed: 23744777
DOI: 10.1126/SCIENCE.1232322

Experimental method

X-RAY DIFFRACTION (2.91 Å)