Structure of the unique SEFIR domain from human interleukin 17 receptor A reveals a composite ligand-binding site containing a conserved α-helix for Act1 binding and IL-17 signaling.

Zhang, Bing

Structure of the unique SEFIR domain from human interleukin 17 receptor A reveals a composite ligand-binding site containing a conserved α-helix for Act1 binding and IL-17 signaling. [electronic resource] - Acta crystallographica. Section D, Biological crystallography May 2014 - 1476-83 p. digital

Publication Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't

1399-0047

10.1107/S1399004714005227 doi


Adaptor Proteins, Signal Transducing
Amino Acid Motifs
Amino Acid Sequence
Binding Sites
Conserved Sequence
Crystallography, X-Ray
Humans
Interleukin-17--metabolism
Ligands
Mutation
Protein Structure, Tertiary
Receptors, Interleukin-17--chemistry
Signal Transduction
Tumor Necrosis Factor Receptor-Associated Peptides and Proteins--metabolism