3A7C
Crystal structure of TLR2-PE-DTPA complex
Summary for 3A7C
| Entry DOI | 10.2210/pdb3a7c/pdb |
| Related | 3A79 3A7B |
| Descriptor | Toll-like receptor 2, Variable lymphocyte receptor B, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total) |
| Functional Keywords | toll-like receptor, pe-dtpa, leucine rich repeat, cell membrane, cytoplasmic vesicle, disulfide bond, glycoprotein, immune response, inflammatory response, membrane, receptor, transmembrane, phosphoprotein, immune system |
| Biological source | Mus musculus (mouse, Inshore hagfish) More |
| Total number of polymer chains | 1 |
| Total formula weight | 67953.61 |
| Authors | Kang, J.Y.,Jin, M.S.,Lee, J.-O. (deposition date: 2009-09-20, release date: 2009-11-24, Last modification date: 2024-10-23) |
| Primary citation | Kang, J.Y.,Nan, X.,Jin, M.S.,Youn, S.-J.,Ryu, Y.H.,Mah, S.,Han, S.H.,Lee, H.,Paik, S.-G.,Lee, J.-O. Recognition of lipopeptide patterns by Toll-like receptor 2-Toll-like receptor 6 heterodimer Immunity, 31:873-884, 2009 Cited by PubMed Abstract: Toll-like receptor 2 (TLR2) initiates potent immune responses by recognizing diacylated and triacylated lipopeptides. Its ligand specificity is controlled by whether it heterodimerizes with TLR1 or TLR6. We have determined the crystal structures of TLR2-TLR6-diacylated lipopeptide, TLR2-lipoteichoic acid, and TLR2-PE-DTPA complexes. PE-DTPA, 1,2-dimyristoyl-sn-glycero-3-phosphoethanolamine-N-diethylenetriaminepentaacetic acid, is a synthetic phospholipid derivative. Two major factors contribute to the ligand specificity of TLR2-TLR1 or TLR2-TLR6 heterodimers. First, the lipid channel of TLR6 is blocked by two phenylalanines. Simultaneous mutation of these phenylalanines made TLR2-TLR6 fully responsive not only to diacylated but also to triacylated lipopeptides. Second, the hydrophobic dimerization interface of TLR2-TLR6 is increased by 80%, which compensates for the lack of amide lipid interaction between the lipopeptide and TLR2-TLR6. The structures of the TLR2-lipoteichoic acid and the TLR2-PE-DTPA complexes demonstrate that a precise interaction pattern of the head group is essential for a robust immune response by TLR2 heterodimers. PubMed: 19931471DOI: 10.1016/j.immuni.2009.09.018 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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