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, B.; Liu, C.; Qian, W.; Han, Y.; Li, X.; Deng, J.

doi:10.1107/S1399004714005227

Acta Crystallographica Section D
Acta Crystallographica
Section D STRUCTURAL BIOLOGY

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Figure 2
Helix αB′ is tethered to helices αB and αC via hydrophobic and hydrogen-bonding interactions. The side chains of the hydrophobic residues are shown as sticks with dotted spheres showing the van der Waals radius for each atom. The hydrogen bond between N^∊1 of Trp428 and O^∊1 of Glu416 is shown as a purple dashed line.

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

Volume 70| Part 5| May 2014| Pages 1476-1483

https://doi.org/10.1107/S1399004714005227

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