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.

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Detalles Bibliográficos
Autores principales: 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
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2021
Materias:
Science
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Acceso en línea:https://doaj.org/article/c6fcc1c1f3344e70a63c5dfee1ef2786
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Descripción
Sumario: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.

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