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• W2057961314 abstract "Abstract Suppressors of cytokine signaling (SOCS) proteins function as negative regulators of cytokine signaling and are involved in fine tuning the immune response. The structure and role of the SH2 domains and C‐terminal SOCS box motifs of the SOCS proteins are well characterized, but the long N‐terminal domains of SOCS4–7 remain poorly understood. Here, we present bioinformatic analyses of the N‐terminal domains of the mammalian SOCS proteins, which indicate that these domains of SOCS4, 5, 6, and 7 are largely disordered. We have also identified a conserved region of about 70 residues in the N‐terminal domains of SOCS4 and 5 that is predicted to be more ordered than the surrounding sequence. The conservation of this region can be traced as far back as lower vertebrates. As conserved regions with increased structural propensity that are located within long disordered regions often contain molecular recognition motifs, we expressed the N‐terminal conserved region of mouse SOCS4 for further analysis. This region, mSOCS4 86–155 , has been characterized by circular dichroism and nuclear magnetic resonance spectroscopy, both of which indicate that it is predominantly unstructured in aqueous solution, although it becomes helical in the presence of trifluoroethanol. The high degree of sequence conservation of this region across different species and between SOCS4 and SOCS5 nonetheless implies that it has an important functional role, and presumably this region adopts a more ordered conformation in complex with its partners. The recombinant protein will be a valuable tool in identifying these partners and defining the structures of these complexes. Proteins 2011. © 2012 Wiley Periodicals, Inc." @default.
• W2057961314 created "2016-06-24" @default.
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• W2057961314 creator A5039797008 @default.
• W2057961314 creator A5059368847 @default.
• W2057961314 date "2011-12-23" @default.
• W2057961314 modified "2023-10-12" @default.
• W2057961314 title "The N-terminal domains of SOCS proteins: A conserved region in the disordered N-termini of SOCS4 and 5" @default.
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• W2057961314 doi "https://doi.org/10.1002/prot.23252" @default.
• W2057961314 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/22423360" @default.
• W2057961314 hasPublicationYear "2011" @default.
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