Conservative Tryptophan Mutants of the Protein Tyrosine Phosphatase YopH Exhibit Impaired WPD-Loop Function and Crystallize with Divanadate Esters in Their Active Sites-Reference-Cited by-同舟云学术

Conservative Tryptophan Mutants of the Protein Tyrosine Phosphatase YopH Exhibit Impaired WPD-Loop Function and Crystallize with Divanadate Esters in Their Active Sites

Published:2015-10-14 Issue:42 Volume:54 Page:6490-6500
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Moise Gwendolyn¹,Gallup Nathan M.²,Alexandrova Anastassia N.²³,Hengge Alvan C.¹,Johnson Sean J.¹

Affiliation:

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

2. Department of Chemistry and Biochemistry, University of California, Los Angeles, California 90095-1569, United States

3. California Nanosystems Institute, University of California, Los Angeles, California 90095-1569, United States

Funder

Division of Chemistry

Division of Biological Infrastructure

National Institutes of Health

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.5b00496

Reference71 articles.

1. Protein kinases and phosphatases: The Yin and Yang of protein phosphorylation and signaling

2. Molecular Reactions of Protein PhosphatasesInsights from Structure and Chemistry

3. Protein-tyrosine phosphatases: Structure, mechanism, and inhibitor discovery

4. Protein Tyrosine Phosphatases in the Human Genome

5. Factors promoting acute and chronic diseases caused by yersiniae

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