6LW5
Crystal structure of the human formyl peptide receptor 2 in complex with WKYMVm
Summary for 6LW5
| Entry DOI | 10.2210/pdb6lw5/pdb |
| Descriptor | Soluble cytochrome b562,N-formyl peptide receptor 2, TRP-LYS-TYR-MET-VAL-QXV, CHOLESTEROL, ... (4 entities in total) |
| Functional Keywords | formyl peptide receptor, g protein-coupled receptor, complex, peptide agonist, membrane protein |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 2 |
| Total formula weight | 49324.44 |
| Authors | |
| Primary citation | Chen, T.,Xiong, M.,Zong, X.,Ge, Y.,Zhang, H.,Wang, M.,Won Han, G.,Yi, C.,Ma, L.,Ye, R.D.,Xu, Y.,Zhao, Q.,Wu, B. Structural basis of ligand binding modes at the human formyl peptide receptor 2. Nat Commun, 11:1208-1208, 2020 Cited by PubMed Abstract: The human formyl peptide receptor 2 (FPR2) plays a crucial role in host defense and inflammation, and has been considered as a drug target for chronic inflammatory diseases. A variety of peptides with different structures and origins have been characterized as FPR2 ligands. However, the ligand-binding modes of FPR2 remain elusive, thereby limiting the development of potential drugs. Here we report the crystal structure of FPR2 bound to the potent peptide agonist WKYMVm at 2.8 Å resolution. The structure adopts an active conformation and exhibits a deep ligand-binding pocket. Combined with mutagenesis, ligand binding and signaling studies, key interactions between the agonist and FPR2 that govern ligand recognition and receptor activation are identified. Furthermore, molecular docking and functional assays reveal key factors that may define binding affinity and agonist potency of formyl peptides. These findings deepen our understanding about ligand recognition and selectivity mechanisms of the formyl peptide receptor family. PubMed: 32139677DOI: 10.1038/s41467-020-15009-1 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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