Discovery of an exosite on the SOCS2-SH2 domain that enhances SH2 binding to phosphorylated ligands

Discovery of an exosite on the SOCS2-SH2 domain that enhances SH2 binding to phosphorylated ligands

SOCS2 is a key regulator of growth hormone and cytokine signaling, which recognizes phosphotyrosine (pTyr)-modified targets via a central SH2 domain. Here, the authors discover and characterize an exosite on this SH2 domain that can bind a non-phosphorylated peptide to enhance SOCS2:pTyr affinity.

Saved in:
Bibliographic Details
Main Authors: Edmond M. Linossi, Kunlun Li, Gianluca Veggiani, Cyrus Tan, Farhad Dehkhoda, Colin Hockings, Dale J. Calleja, Narelle Keating, Rebecca Feltham, Andrew J. Brooks, Shawn S. Li, Sachdev S. Sidhu, Jeffrey J. Babon, Nadia J. Kershaw, Sandra E. Nicholson
Format: article
Language:EN
Published: Nature Portfolio 2021
Subjects:
Science
Q
Online Access:https://doaj.org/article/c6fcc1c1f3344e70a63c5dfee1ef2786
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:SOCS2 is a key regulator of growth hormone and cytokine signaling, which recognizes phosphotyrosine (pTyr)-modified targets via a central SH2 domain. Here, the authors discover and characterize an exosite on this SH2 domain that can bind a non-phosphorylated peptide to enhance SOCS2:pTyr affinity.

Similar Items