Conformational changes in human prolyl-tRNA synthetase upon binding of the substrates proline and ATP and the inhibitor halofuginone

Acta Crystallographica Section D: Biological Crystallography

Volumn 69, Issue 10, 2013, Pages 2136-2145

  Son, Jonghyeon ^a   Lee, Eun Hye ^a   Park, Minyoung ^b,c   Kim, Jong Hyun ^b,c   Kim, Junsoo ^a   Kim, Sunghoon ^b,c   Jeon, Young Ho ^a   Hwang, Kwang Yeon ^a  

^a Korea University   (South Korea)

^b Seoul National University   (South Korea)

^c Seoul National University   (South Korea)

Author keywords

drug design; glutamyl prolyl tRNA synthetase; herbal inhibitor; inflammation; multisynthetase complex

Indexed keywords

ADENOSINE TRIPHOSPHATE; AMINO ACID TRANSFER RNA LIGASE; GLUTAMATE TRANSFER RNA LIGASE; HALOFUGINONE; PIPERIDINE DERIVATIVE; PROLINE; PROLYL T RNA SYNTHETASE; PROTEIN SYNTHESIS INHIBITOR; QUINAZOLINONE DERIVATIVE;

ARTICLE; CHEMISTRY; DRUG ANTAGONISM; DRUG DESIGN; DRUG EFFECT; ENZYME ACTIVE SITE; ENZYME SPECIFICITY; GENETICS; GLUTAMYL-PROLYL-TRNA SYNTHETASE; HERBAL INHIBITOR; HUMAN; INFLAMMATION; MULTISYNTHETASE COMPLEX; MUTAGENESIS; PROTEIN BINDING; PROTEIN CONFORMATION; X RAY CRYSTALLOGRAPHY;

DRUG DESIGN; GLUTAMYL-PROLYL-TRNA SYNTHETASE; HERBAL INHIBITOR; INFLAMMATION; MULTISYNTHETASE COMPLEX;

ADENOSINE TRIPHOSPHATE; AMINO ACYL-TRNA SYNTHETASES; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; GLUTAMATE-TRNA LIGASE; HUMANS; MUTAGENESIS; PIPERIDINES; PROLINE; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN SYNTHESIS INHIBITORS; QUINAZOLINONES; SUBSTRATE SPECIFICITY;

EID: 84885460185     PISSN: 09074449     EISSN: 13990047     Source Type: Journal    
DOI: 10.1107/S0907444913020556     Document Type: Article

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