Schön et al. reply to 'Efomycine M: an inhibitor of selectins?'

Autor:	Gesche Harms, Sven Enders, Ralf Ludwig, Michael P. Schön, Bernd Kramer, Gertie J. Oostingh, B. Gregor Wienrich, Rudolf Tauber, W. Henning Boehncke, Thomas Krahn
Rok vydání:	2006
Předmět:	Chemistry Stereochemistry Binding pocket General Medicine Pharmacophore General Biochemistry Genetics and Molecular Biology In vitro binding Efomycine M Selectin
Zdroj:	Nature Medicine. 12:873-874
ISSN:	1546-170X 1078-8956
DOI:	10.1038/nm0806-873b
Popis:	The hypothesis raised by von Bonin et al. is an interesting extension of our previous findings. However, the single previously known hydrogen bond within the efomycine molecule does not exclude the pharmacophore hypothesis, and the use of artificial selectin molecules for in vitro binding studies needs to be evaluated further. Our own recent report proposes a substantially refined model of efomycine M binding1, 2. Although apparently not taken into consideration by von Bonin et al., these results predict a different orientation and stronger binding of efomycine M (Efo-M) within the binding pocket of E-selectin as compared to sLeX, a weak binder3, thus providing a potential explanation for the observation that Efo-M binding could not be competitively inhibited by sLeX.
Databáze:	OpenAIRE
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