NMR structure of a potent small molecule inhibitor bound to human keratinocyte fatty acid-binding protein.

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McDonnell PA, Constantine KL, Goldfarb V, Johnson SR, Sulsky R, Magnin DR, Robl JA, Caulfield TJ, Parker RA, Taylor DS, Adam LP, Metzler WJ, Mueller L, Farmer BT 2nd

NMR structure of a potent small molecule inhibitor bound to human keratinocyte fatty acid-binding protein.

J Med Chem. 2006 Aug 10;49(16):5013-7.

PubMed ID

16884313 [ View in PubMed

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Abstract

The NMR structure is presented for compound 1 (BMS-480404) (Ki = 33 (+/-2) nM) bound to keratinocyte fatty acid-binding protein. This article describes interactions between a high affinity drug-like compound and a member of the fatty acid-binding protein family. A benzyl group ortho to the mandelic acid in 1 occupies an area of the protein that fatty acids do not normally contact. Similar to that in the kFABP-palmitic acid structure, the acid moiety in 1 is proximal to R129 and Y131. Computational modeling indicates that the acid moiety in 1 interacts indirectly via a modeled water molecule to R109.

DrugBank Data that Cites this Article

Binding Properties

Drug	Target	Property	Measurement	pH	Temperature (°C)
Palmitic Acid	Fatty acid-binding protein, epidermal	Kd (nM)	802	N/A	N/A	Details