A substrate variant as a high-affinity, reversible inhibitor: Insight from the X-ray structure of cilastatin bound to membrane dipeptidase

Bioorganic and Medicinal Chemistry

Volumn 11, Issue 6, 2003, Pages 991-998

  Smyth, Timothy P ^a   Wall, J Gerard ^a   Nitanai, Yasushi ^b,c  

^a UNIVERSITY OF LIMERICK   (Ireland)

^b SUNTORY LTD   (Japan)

^c RIKEN   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

AMIDE; AMINO ACID; CILASTATIN; DIPEPTIDASE; ENZYME INHIBITOR; HYDROXIDE; MEMBRANE ENZYME; WATER; ZINC;

ARTICLE; BINDING AFFINITY; BINDING SITE; CHEMICAL BOND; CHEMICAL REACTION; CRYSTAL STRUCTURE; DRUG BINDING; DRUG PROTEIN BINDING; DRUG STRUCTURE; ENZYME SUBSTRATE; PROTEIN STRUCTURE; STRUCTURE ANALYSIS; X RAY ANALYSIS;

AMIDOHYDROLASES; CHEMISTRY, PHYSICAL; CILASTATIN; CRYSTALLOGRAPHY, X-RAY; DIPEPTIDASES; ENZYME INHIBITORS; LEUKOTRIENE D4; MODELS, MOLECULAR; PROTEIN BINDING; PROTEIN CONFORMATION;

EID: 0037334067     PISSN: 09680896     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0968-0896(02)00519-9     Document Type: Article

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40. The other docked conformers had the same general orientation as that shown here, however, these were not as closely aligned as the set shown for cilastatin in Figure 6.
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