Literature summary for 3.4.23.B5 extracted from

Furukawa, A.; Okamura, H.; Morishita, R.; Matsunaga, S.; Kobayashi, N.; Ikegami, T.; Kodaki, T.; Takaori-Kondo, A.; Ryo, A.; Nagata, T.; Katahira, M.
NMR study of xenotropic murine leukemia virus-related virus protease in a complex with amprenavir (2012), Biochem. Biophys. Res. Commun., 425, 284-289.

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Inhibitors

Inhibitors	Comment	Organism	Structure
amprenavir	NMR structural analysis of recombinant protease in complex with amprenavir. One amprenavir molecule binds to one protease dimer. Intermolecular NOE signals between amprenavir and either the methyl groups of A35, V39, V54, A57, L83 and L92 or the aromatic ring of Y90 can be identified. The structural heterogeneity induced by the asymmetry of the binding of amprenavir to the protease dimer is transmitted to distant regions	Xenotropic MuLV-related virus

Organism

Organism	UniProt	Comment	Textmining
Xenotropic MuLV-related virus	A1Z651	Gag-Pol polyprotein	-
Xenotropic MuLV-related virus isolate VP62	A1Z651	Gag-Pol polyprotein	-

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Release 2023.1 (January 2023)