Crystal structures of STING protein reveal basis for recognition of cyclic di-GMP
G Shang, D Zhu, N Li, J Zhang, C Zhu, D Lu… - Nature structural & …, 2012 - nature.com
G Shang, D Zhu, N Li, J Zhang, C Zhu, D Lu, C Liu, Q Yu, Y Zhao, S Xu, L Gu
Nature structural & molecular biology, 2012•nature.comSTING functions as both an adaptor protein signaling cytoplasmic double-stranded DNA and
a direct immunosensor of cyclic diguanylate monophosphate (c-di-GMP). The crystal
structures of the C-terminal domain of human STING (STINGCTD) and its complex with c-di-
GMP reveal how STING recognizes c-di-GMP. In response to c-di-GMP binding, two surface
loops, which serve as a gate and latch of the cleft formed by the dimeric STINGCTD,
undergo rearrangements to interact with the ligand.
a direct immunosensor of cyclic diguanylate monophosphate (c-di-GMP). The crystal
structures of the C-terminal domain of human STING (STINGCTD) and its complex with c-di-
GMP reveal how STING recognizes c-di-GMP. In response to c-di-GMP binding, two surface
loops, which serve as a gate and latch of the cleft formed by the dimeric STINGCTD,
undergo rearrangements to interact with the ligand.
Abstract
STING functions as both an adaptor protein signaling cytoplasmic double-stranded DNA and a direct immunosensor of cyclic diguanylate monophosphate (c-di-GMP). The crystal structures of the C-terminal domain of human STING (STINGCTD) and its complex with c-di-GMP reveal how STING recognizes c-di-GMP. In response to c-di-GMP binding, two surface loops, which serve as a gate and latch of the cleft formed by the dimeric STINGCTD, undergo rearrangements to interact with the ligand.
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