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PDBsum entry 6lw5
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Membrane protein
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PDB id
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6lw5
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References listed in PDB file
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Key reference
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Title
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Structural basis of ligand binding modes at the human formyl peptide receptor 2.
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Authors
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T.Chen,
M.Xiong,
X.Zong,
Y.Ge,
H.Zhang,
M.Wang,
G.Won han,
C.Yi,
L.Ma,
R.D.Ye,
Y.Xu,
Q.Zhao,
B.Wu.
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Ref.
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Nat Commun, 2020,
11,
1208.
[DOI no: ]
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PubMed id
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Abstract
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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.
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