The dynamics of signal triggering in a gp130-receptor complex.
gp130 is a shared signal-transducing membrane-associated receptor for several hematopoietic cytokines. The 30 A resolution cryo-electron microscopy (cryo-EM) structure of the Interleukin 11(IL-11)-IL-11 Receptor-gp130 extracellular complex reveals the architecture and dynamics of this gp130-containing signaling complex. Normal-mode analysis reveals a repertoire of conformational changes that could function in signal triggering. This suggests a concerted mechanism of signaling involving all the components of the complex. This could provide a general mechanism of signal transfer for cytokines utilizing the JAK-STAT signaling cascade.
Matadeen
Rishi
R
Division of Structural Biology, The Wellcome Trust Centre for Human Genetics, University of Oxford, Roosevelt Drive, Headington, Oxford OX3 7BN, United Kingdom. rishi@strubi.ox.ac.uk <rishi@strubi.ox.ac.uk>
Hon
Wai-Ching
WC
Heath
John K
JK
Jones
E Yvonne
EY
Fuller
Stephen
S
D000818:Animals; D020285:Cryoelectron Microscopy; D050822:Cytokine Receptor gp130 / Q000737:chemistry / Q000378:metabolism*; D017370:Interleukin-11 / Q000737:chemistry / Q000502:physiology*; D051379:Mice; D011485:Protein Binding; D053702:Receptors, Interleukin-11 / Q000737:chemistry / Q000378:metabolism*; D015398:Signal Transduction / Q000502:physiology*
C494200:Il6st protein, mouse; D017370:Interleukin-11; D053702:Receptors, Interleukin-11; D050822:Cytokine Receptor gp130