2LMB

Solution Structure of C-terminal RAGE (ctRAGE)

Summary for 2LMB

• Entry DOI: 10.2210/pdb2lmb/pdb
• NMR Information: BMRB: 18110
• Descriptor: Advanced glycosylation end product-specific receptor (1 entity in total)
• Functional Keywords: signal transduction receptor, cytosolic tail, signaling protein
• Biological source: Homo sapiens (human)
• Cellular location: Isoform 1: Cell membrane; Single-pass type I membrane protein. Isoform 2: Secreted. Isoform 10: Cell membrane ; Single-pass type I membrane protein : Q15109
• Total number of polymer chains: 1
• Total formula weight: 5035.24

Authors

Rai, V.,Maldonado, A.Y.,Burz, D.S.,Reverdatto, S.,Schmidt, A.,Shekhtman, A. (deposition date: 2011-11-29, release date: 2011-12-21, Last modification date: 2024-05-15)

Primary citation

Rai, V.,Maldonado, A.Y.,Burz, D.S.,Reverdatto, S.,Schmidt, A.M.,Shekhtman, A.
Signal transduction in receptor for advanced glycation end products (RAGE): solution structure of C-terminal rage (ctRAGE) and its binding to mDia1.
J.Biol.Chem., 287:5133-5144, 2012

PubMed Abstract: The receptor for advanced glycation end products (RAGE) is a multiligand cell surface macromolecule that plays a central role in the etiology of diabetes complications, inflammation, and neurodegeneration. The cytoplasmic domain of RAGE (C-terminal RAGE; ctRAGE) is critical for RAGE-dependent signal transduction. As the most membrane-proximal event, mDia1 binds to ctRAGE, and it is essential for RAGE ligand-stimulated phosphorylation of AKT and cell proliferation/migration. We show that ctRAGE contains an unusual α-turn that mediates the mDia1-ctRAGE interaction and is required for RAGE-dependent signaling. The results establish a novel mechanism through which an extracellular signal initiated by RAGE ligands regulates RAGE signaling in a manner requiring mDia1.

PubMed: 22194616
DOI: 10.1074/jbc.M111.277731

Experimental method

SOLUTION NMR