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2IZV

CRYSTAL STRUCTURE OF SOCS-4 IN COMPLEX WITH ELONGIN-B AND ELONGIN-C AT 2.55A RESOLUTION

Summary for 2IZV
Entry DOI10.2210/pdb2izv/pdb
Related1LM8 1LQB 1VCB 2C9W
DescriptorSUPPRESSOR OF CYTOKINE SIGNALING 4, TRANSCRIPTION ELONGATION FACTOR B POLYPEPTIDE 2, TRANSCRIPTION ELONGATION FACTOR B POLYPEPTIDE 1, ... (7 entities in total)
Functional Keywordssignal transduction inhibitor, growth regulation, signal transduction, sh2 domain, transcription, nuclear protein, ubl conjugation pathway, transcription regulation
Biological sourceHOMO SAPIENS (HUMAN)
More
Total number of polymer chains3
Total formula weight45979.62
Authors
Debreczeni, J.E.,Bullock, A.,Papagrigoriou, E.,Turnbull, A.,Pike, A.C.W.,Gorrec, F.,von Delft, F.,Sundstrom, M.,Arrowsmith, C.,Weigelt, J.,Edwards, A.,Knapp, S. (deposition date: 2006-07-26, release date: 2006-08-02, Last modification date: 2023-12-13)
Primary citationBullock, A.N.,Rodriguez, M.C.,Debreczeni, J.E.,Songyang, Z.,Knapp, S.
Structure of the SOCS4-ElonginB/C complex reveals a distinct SOCS box interface and the molecular basis for SOCS-dependent EGFR degradation.
Structure, 15:1493-1504, 2007
Cited by
PubMed Abstract: Tyrosine kinase signaling is tightly controlled by negative feedback inhibitors including suppressors of cytokine signaling (SOCS). SOCS assemble as SH2 domain substrate recognition modules in ElonginB/C-cullin ubiquitin ligases. In accordance, SOCS4 reduces STAT3 signaling from EGFR through increased receptor degradation. Variable C-termini in SOCS4-SOCS7 exclude these family members from a SOCS2-type domain arrangement in which a strictly conserved C terminus determines domain packing. The structure of the SOCS4-ElonginC-ElonginB complex reveals a distinct SOCS structural class. The N-terminal ESS helix functionally replaces the CIS/SOCS1-SOCS3 family C terminus in a distinct SH2-SOCS box interface that facilitates further interdomain packing between the extended N- and C-terminal regions characteristic for this subfamily. Using peptide arrays and calorimetry the STAT3 site in EGFR (pY(1092)) was identified as a high affinity SOCS4 substrate (K(D) = 0.5 microM) revealing a mechanism for EGFR degradation. SOCS4 also bound JAK2 and KIT with low micromolar affinity, whereas SOCS2 was specific for GH-receptor.
PubMed: 17997974
DOI: 10.1016/j.str.2007.09.016
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.55 Å)
Structure validation

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