Fig. 4 | Nature Communications

Fig. 4

From: The molecular basis of JAK/STAT inhibition by SOCS1

Fig. 4

Structure of the SOCS1–Elongin B/C complex. a Structure of Xenopus laevis SOCS1 (red) in complex with Elongin B (pale green) and Elongin C (green). b The SOCS1 SOCS Box is shown overlaid with the structure of SOCS2 (cyan) bound to Cullin5 (blue). SOCS1 Asn197 takes the place of terminal proline typically seen in the canonical Cullin5 binding motif (LPφP). This asparagine clashes with Trp53 of Cullin5. Likewise, the Arg186 (SOCS2)-Thr117 (Cul5) hydrogen bond is lost in SOCS1 which has a valine (Val200) in place of the arginine. c Model of the JAK1-SOCS1-Elongin B/C-Cullin5-Rbx2 (white) complex based upon the SOCS1/JAK1 (this manuscript), SOCS2/ElonginB/ElonginC/Cullin5 NTD (PDB: 4JGH) and Cul5 CTD/Rbx2 structures (PDB: 3DPL). The SOCS1/JAK1 interaction orients JAK1 toward rbx2, which is the site of activated-ubiquitin (ubiquitin-E2) binding

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