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2N34

NMR assignments and solution structure of the JAK interaction region of SOCS5

Replaces:  2MP6
Summary for 2N34
Entry DOI10.2210/pdb2n34/pdb
NMR InformationBMRB: 19966
DescriptorSuppressor of cytokine signaling 5 (1 entity in total)
Functional Keywordssuppressor of cytokine signalling, jak interaction region, intrinsically unstructured protein, signaling protein
Biological sourceMus musculus (mouse)
Total number of polymer chains1
Total formula weight8116.52
Authors
Chandrashekaran, I.R.,Mohanty, B.,Linossi, E.M.,Nicholson, S.E.,Babon, J.,Norton, R.S.,Dagley, L.F.,Leung, E.W.W.,Murphy, J.M. (deposition date: 2015-05-21, release date: 2015-07-29, Last modification date: 2024-05-15)
Primary citationChandrashekaran, I.R.,Mohanty, B.,Linossi, E.M.,Dagley, L.F.,Leung, E.W.,Murphy, J.M.,Babon, J.J.,Nicholson, S.E.,Norton, R.S.
Structure and Functional Characterization of the Conserved JAK Interaction Region in the Intrinsically Disordered N-Terminus of SOCS5.
Biochemistry, 54:4672-4682, 2015
Cited by
PubMed Abstract: SOCS5 can negatively regulate both JAK/STAT and EGF-receptor pathways and has therefore been implicated in regulating both the immune response and tumorigenesis. Understanding the molecular basis for SOCS5 activity may reveal novel ways to target key components of these signaling pathways. The N-terminal region of SOCS5 coordinates critical protein interactions involved in inhibition of JAK/STAT signaling, and a conserved region within the N-terminus of SOCS5 mediates direct binding to the JAK kinase domain. Here we have characterized the solution conformation of this conserved JAK interaction region (JIR) within the largely disordered N-terminus of SOCS5. Using nuclear magnetic resonance (NMR) chemical shift analysis, relaxation measurements, and NOE analysis, we demonstrate the presence of preformed structural elements in the JIR of mouse SOCS5 (mSOCS5175-244), consisting of an α-helix encompassing residues 224-233, preceded by a turn and an extended structure. We have identified a phosphorylation site (Ser211) within the JIR of mSOCS5 and have investigated the role of phosphorylation in modulating JAK binding using site-directed mutagenesis.
PubMed: 26173083
DOI: 10.1021/acs.biochem.5b00619
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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