Identification and characterization of a large family of superbinding bacterial SH2 domains
SH2 domains bind to tyrosine-phosphorylated proteins and play crucial roles in signal transduction in mammalian cells. Here, Kaneko et al. identify a large family of SH2 domains in the bacterial pathogen Legionella that bind to mammalian phosphorylated proteins, in some cases with very high affinity...
Saved in:
Main Authors: | Tomonori Kaneko, Peter J. Stogios, Xiang Ruan, Courtney Voss, Elena Evdokimova, Tatiana Skarina, Amy Chung, Xiaoling Liu, Lei Li, Alexei Savchenko, Alexander W. Ensminger, Shawn S.-C. Li |
---|---|
Format: | article |
Language: | EN |
Published: |
Nature Portfolio
2018
|
Subjects: | |
Online Access: | https://doaj.org/article/4802b25f8b354260bed6a583ba5257d2 |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Similar Items
-
The evolution of substrate discrimination in macrolide antibiotic resistance enzymes
by: Andrew C. Pawlowski, et al.
Published: (2018) -
Discovery of an exosite on the SOCS2-SH2 domain that enhances SH2 binding to phosphorylated ligands
by: Edmond M. Linossi, et al.
Published: (2021) -
Structural and Functional Adaptation of Vancomycin Resistance VanT Serine Racemases
by: Djalal Meziane-Cherif, et al.
Published: (2015) -
ApmA Is a Unique Aminoglycoside Antibiotic Acetyltransferase That Inactivates Apramycin
by: Emily Bordeleau, et al.
Published: (2021) -
SH3 domain tyrosine phosphorylation--sites, role and evolution.
by: Zuzana Tatárová, et al.
Published: (2012)