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Solution structure of the low-molecular-weight protein tyrosine phosphatase from Tritrichomonas foetus reveals a flexible phosphate binding loop

Eukaryotic low-molecular-weight protein tyrosine phosphatases (LMW PTPs) contain a conserved serine, a histidine with an elevated pK(a), and an active site asparagine that together form a highly conserved hydrogen bonding network. This network stabilizes the active site phosphate binding loop for op...

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Bibliographic Details
Main Authors: Gustafson, Christin L.T., Stauffacher, Cynthia V., Hallenga, Klaas, Van Etten, Robert L.
Format: Artigo
Language:Inglês
Published: Cold Spring Harbor Laboratory Press 2005
Subjects:
Online Access:https://ncbi.nlm.nih.gov/pmc/articles/PMC2253298/
https://ncbi.nlm.nih.gov/pubmed/16195543
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1110/ps.051618805
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