Trimeric structure of PRL-1 phosphatase reveals an active enzyme conformation and regulation mechanisms

Journal of Molecular Biology

Volumn 345, Issue 2, 2005, Pages 401-413

  Jeong, Dae Gwin ^a   Kim, Seung Jun ^a   Kim, Jae Hoon ^a   Son, Jeong Hee ^a   Park, Mi Rim ^a   Lim, Sang Myoun ^a   Yoon, Tae Sung ^a   Ryu, Seong Eon ^a  

^a Korea Research Institute of Bioscience and Biotechnology (KRIBB)   (South Korea)

Author keywords

active form; crystal structure; metastasis inhibitor; oligomerization; PRL phosphatases

Indexed keywords

ISOENZYME; PHOSPHATASE OF REGENERATING LIVER 1; PHOSPHATASE OF REGENERATING LIVER 3; PROTEIN TYROSINE PHOSPHATASE; UNCLASSIFIED DRUG;

ARTICLE; CELL FRACTIONATION; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME CONFORMATION; ENZYME KINETICS; ENZYME MECHANISM; ENZYME REGULATION; ENZYME STABILITY; ENZYME STRUCTURE; ISOENZYME ANALYSIS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN FAMILY; PROTEIN INTERACTION; STRUCTURAL HOMOLOGY; STRUCTURE ANALYSIS;

EID: 9644295701     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.10.061     Document Type: Article

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