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The diamond anniversary of tissue transglutaminase: a protein of many talents.


ABSTRACT: Tissue transglutaminase (tTG) is capable of binding and hydrolyzing GTP, as well as catalyzing an enzymatic transamidation reaction that crosslinks primary amines to glutamine residues. tTG adopts two vastly different conformations, depending on whether it is functioning as a GTP-binding protein or a crosslinking enzyme. It has been shown to have important roles in several different aspects of cancer progression, making it an attractive target for therapeutic intervention. Here, we highlight many of the major findings involving tTG since its discovery 60 years ago, and describe recent drug discovery efforts that target specific activities or conformations of this unique protein.

SUBMITTER: Katt WP 

PROVIDER: S-EPMC5864117 | biostudies-literature | 2018 Mar

REPOSITORIES: biostudies-literature

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The diamond anniversary of tissue transglutaminase: a protein of many talents.

Katt William P WP   Antonyak Marc A MA   Cerione Richard A RA  

Drug discovery today 20180131 3


Tissue transglutaminase (tTG) is capable of binding and hydrolyzing GTP, as well as catalyzing an enzymatic transamidation reaction that crosslinks primary amines to glutamine residues. tTG adopts two vastly different conformations, depending on whether it is functioning as a GTP-binding protein or a crosslinking enzyme. It has been shown to have important roles in several different aspects of cancer progression, making it an attractive target for therapeutic intervention. Here, we highlight man  ...[more]

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