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Ligand docking in the gastric H+/K+-ATPase: homology modeling of reversible inhibitor binding sites.

Abstract:

Using the recent high-resolution X-ray structures determined for the Ca2+-ATPase, we have generated two homology models of the gastric H+/K+-ATPase reflecting the E1 and E2 conformations adopted by P-type ATPases in their catalytic cycle. In regimes where the in situ solid-state NMR-determined structure for 1,2,3-trimethyl-8-(pentafluorophenylmethoxy)imidazo[1,2-a]pyridinium iodide (TMPFPIP), a reversible inhibitor of the gastric H+/K+-ATPase, was retained in its predefined conformation and w...

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Publication status:
Published

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Publisher copy:
10.1021/jm050326o

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Institution:
University of Oxford
Department:
Oxford, MSD, Biochemistry
Journal:
Journal of medicinal chemistry
Volume:
48
Issue:
23
Pages:
7145-7152
Publication date:
2005-11-05
DOI:
EISSN:
1520-4804
ISSN:
0022-2623
URN:
uuid:575758a7-76e9-47a7-9793-70d412876623
Source identifiers:
100289
Local pid:
pubs:100289

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