Insights into the importance of WPD-loop sequence for activity and structure in protein tyrosine phosphatases

Author:

Shen Ruidan1,Crean Rory M.2,Olsen Keith J.1,Corbella Marina2ORCID,Calixto Ana R.2,Richan Teisha1,Brandão Tiago A. S.3,Berry Ryan D.1,Tolman Alex1,Loria J. Patrick45,Johnson Sean J.1ORCID,Kamerlin Shina C. L.26ORCID,Hengge Alvan C.1ORCID

Affiliation:

1. Department of Chemistry and Biochemistry, Utah State University, Logan, Utah 84322-0300, USA

2. Science for Life Laboratory, Department of Chemistry – BMC, Uppsala University, BMC, Box 576, S-751 23 Uppsala, Sweden

3. Departamento de Química, ICEX, Universidade Federal de Minas Gerais, Belo Horizonte, Minas Gerais, 31270-901, Brazil

4. Department of Chemistry, Yale University, 225 Prospect Street, New Haven, CT 06520, USA

5. Department of Molecular Biophysics and Biochemistry, Yale University, 266 Whitney Avenue, New Haven, CT 06520, USA

6. School of Chemistry and Biochemistry, Georgia Institute of Technology, 901 Atlantic Drive NW, Atlanta, GA 30332-0400, USA

Abstract

Protein tyrosine phosphatases have a key catalytic residue on a mobile loop (the WPD-loop), making the connections between this loop sequence and its dynamics, together with the dynamics of other mobile loops, particularly important.

Funder

National Institutes of Health

Knut och Alice Wallenbergs Stiftelse

Vetenskapsrådet

U.S. Department of Energy

National Institute of General Medical Sciences

Carl Tryggers Stiftelse för Vetenskaplig Forskning

Human Frontier Science Program

National Science Foundation

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemistry

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