Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 53, Issue 49, Pages 13471-13476Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201408246
Keywords
cation-pi interactions; enzyme catalysis; molecular recognition; quaternary ammonium; structural biology
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Funding
- Hungarian Scientific Research Fund [OTKA NK 84008, OTKA K109486]
- Baross program of the New Hungary Development Plan [3DSTRUCT, OMFB-00266/2010 REG-KM-09-1-2009-0050]
- Hungarian Academy of Sciences [TTK IF-28/2012]
- Hungarian Academy of Sciences (MedinProt)
- European Commission FP7 BioStruct-X project [283570]
- Agence Nationale de la Recherche (NKTH ADD-MAL) [ANR-09-BLAN-0397]
- EU FP7/EviMalar NoE [242095]
- Pro Progressio Foundation
- Zsuzsa Szabo Foundation
- Romanian National Authority for Scientific Research, CNCS-UEFISCDI [PN-II-ID-PCE-2011-3-0775]
- Agence Nationale de la Recherche (ANR) [ANR-09-BLAN-0397] Funding Source: Agence Nationale de la Recherche (ANR)
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Cation-pi interactions to cognate ligands in enzymes have key roles in ligand binding and enzymatic catalysis. We have deciphered the key functional role of both charged and aromatic residues within the choline binding subsite of CTP: phosphocholine cytidylyltransferase and choline kinase from Plasmodium falciparum. Comparison of quaternary ammonium binding site structures revealed a general composite aromatic box pattern of enzyme recognition sites, well distinguished from the aromatic box recognition site of receptors.
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