Solution NMR structure and ligand identification of human Gas7 SH3 domain reveal a typical SH3 fold but a non-canonical ligand-binding mode-Reference-Cited by-同舟云学术

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Solution NMR structure and ligand identification of human Gas7 SH3 domain reveal a typical SH3 fold but a non-canonical ligand-binding mode

Published:2019-09 Issue:4 Volume:516 Page:1190-1195
ISSN:0006-291X
Container-title:Biochemical and Biophysical Research Communications
language:en
Short-container-title:Biochemical and Biophysical Research Communications

Author:

Nie Yao,Zhu Jiang,Ramelot Theresa A.^ORCID,Kennedy Michael A.,Liu Maili,He Ting^ORCID,Yang Yunhuang

Funder

National Key R&D Program of China

National Natural Science Foundation of China

National Institute of General Medical Sciences of USA

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry,Biophysics

Reference26 articles.

1. SH3 domains: modules of protein-protein interactions;Kurochkina;Biophys Rev,2013

2. The SH3 domain--a family of versatile peptide- and protein-recognition module;Kaneko;Front. Biosci.,2008

3. SH3 domain ligand binding: what's the consensus and where's the specificity?;Saksela;FEBS Lett.,2012

4. Comprehensive analysis of the human SH3 domain family reveals a wide variety of non-canonical specificities;Teyra;Structure,2017

5. Analysis of mammalian cell genetic regulation in situ by using retrovirus-derived "portable exons" carrying the Escherichia coli lacZ gene;Brenner;Proc. Natl. Acad. Sci. U. S. A.,1989

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