4LIQ
Structure of the extracellular domain of human CSF-1 receptor in complex with the Fab fragment of RG7155
Summary for 4LIQ
Entry DOI | 10.2210/pdb4liq/pdb |
Descriptor | Macrophage colony-stimulating factor 1 receptor, Fab fragment RG7155 heavy chain, Fab fragment RG7155 light chain, ... (8 entities in total) |
Functional Keywords | csf-1 receptor, receptor tyrosine kinase, antibody, fab fragment, igg like domain, immune system |
Biological source | Homo sapiens (human) More |
Total number of polymer chains | 3 |
Total formula weight | 109817.56 |
Authors | Benz, J.,Gorr, I.H.,Hertenberger, H.,Ries, C.H. (deposition date: 2013-07-03, release date: 2014-06-18, Last modification date: 2024-11-20) |
Primary citation | Ries, C.H.,Cannarile, M.A.,Hoves, S.,Benz, J.,Wartha, K.,Runza, V.,Rey-Giraud, F.,Pradel, L.P.,Feuerhake, F.,Klaman, I.,Jones, T.,Jucknischke, U.,Scheiblich, S.,Kaluza, K.,Gorr, I.H.,Walz, A.,Abiraj, K.,Cassier, P.A.,Sica, A.,Gomez-Roca, C.,de Visser, K.E.,Italiano, A.,Le Tourneau, C.,Delord, J.P.,Levitsky, H.,Blay, J.Y.,Ruttinger, D. Targeting tumor-associated macrophages with anti-CSF-1R antibody reveals a strategy for cancer therapy Cancer Cell, 25:846-859, 2014 Cited by PubMed Abstract: Macrophage infiltration has been identified as an independent poor prognostic factor in several cancer types. The major survival factor for these macrophages is macrophage colony-stimulating factor 1 (CSF-1). We generated a monoclonal antibody (RG7155) that inhibits CSF-1 receptor (CSF-1R) activation. In vitro RG7155 treatment results in cell death of CSF-1-differentiated macrophages. In animal models, CSF-1R inhibition strongly reduces F4/80(+) tumor-associated macrophages accompanied by an increase of the CD8(+)/CD4(+) T cell ratio. Administration of RG7155 to patients led to striking reductions of CSF-1R(+)CD163(+) macrophages in tumor tissues, which translated into clinical objective responses in diffuse-type giant cell tumor (Dt-GCT) patients. PubMed: 24898549DOI: 10.1016/j.ccr.2014.05.016 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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