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Protonation states of central amino acids in a zinc metalloprotease complexed with inhibitor: Molecular mechanics optimizations and ab initio molecular orbital calculations

Permanent lenke
https://hdl.handle.net/10037/30934
DOI
https://doi.org/10.1016/j.bpc.2020.106368
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article.pdf (604.3Kb)
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Dato
2020-04-01
Type
Journal article
Tidsskriftartikkel
Peer reviewed

Forfatter
Ezawa, Takuya; Saito, Ryosuke; Suzuki, Shusuke; Sugiyama, Satoshi; Sylte, Ingebrigt; Kurita, Noriyuki
Sammendrag
The zinc-metalloprotease pseudolysin (PLN) secreted from bacteria degrades extracellular proteins to produce bacterial nutrition. Since PLN has a Zn ion at the inhibitor-binding site, the interactions between Zn and PLN residues as well as inhibitor can be significantly changed depending on the protonation states of PLN residues at the inhibitor-binding site. To determine stable protonation states of these residues, we here considered different protonation states for Glu and His residues located around Zn and investigated the electronic states of the PLN + inhibitor complex, using ab initio molecular simulations. The protonation state of His223 was found to significantly affect the specific interactions between PLN and the inhibitor.
Forlag
Elsevier
Sitering
Ezawa T, Saito, Suzuki, Sugiyama S, Sylte IS, Kurita N. Protonation states of central amino acids in a zinc metalloprotease complexed with inhibitor: Molecular mechanics optimizations and ab initio molecular orbital calculations . Biophysical Chemistry. 2020
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  • Artikler, rapporter og annet (medisinsk biologi) [1103]
Copyright 2020 The Author(s)

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