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 5
Val550 is a buried internal residue in IL-17RA SEFIR. The missing fragment (residues 541–555) connecting helices αE and αE′ of the crystal structure was modeled using FALC-Loop (https://falc-loop.seoklab.org/). Residue Val550 is located on helix αM and is buried inside the protein, making extensive hydrophobic contacts with three aromatic residues from helices αA (Phe401), αE (Phe529) and αE′ (Tyr558). The V550H mutation will disrupt the structural integrity.

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

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

https://doi.org/10.1107/S1399004714005227

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