Crystal structure of AmpC BER and molecular docking lead to the discovery of broad inhibition activities of halisulfates against ß-lactamases.

Jeong, Bo-Gyeong; Na, Jung-Hyun; Bae, Da-Woon; Park, Soo-Bong; Lee, Hyi-Seung; Cha, Sun-Shin

Jeong, Bo-Gyeong; Na, Jung-Hyun; Bae, Da-Woon; Park, Soo-Bong; Lee, Hyi-Seung; Cha, Sun-Shin.

Afiliação

Jeong BG; Department of Chemistry & Nanoscience, Ewha Womans University, Seoul 03760, Republic of Korea.
Na JH; Department of Chemistry & Nanoscience, Ewha Womans University, Seoul 03760, Republic of Korea.
Bae DW; Department of Chemistry & Nanoscience, Ewha Womans University, Seoul 03760, Republic of Korea.
Park SB; Department of Chemistry & Nanoscience, Ewha Womans University, Seoul 03760, Republic of Korea.
Lee HS; Marine Natural Products Chemistry Laboratory, Korea Institute of Ocean Science and Technology, Busan 49111, Republic of Korea.
Cha SS; Department of Chemistry & Nanoscience, Ewha Womans University, Seoul 03760, Republic of Korea.

Comput Struct Biotechnol J ; 19: 145-152, 2021.

Article em En | MEDLINE | ID: mdl-33425247

Palavras-chave

AmpC BER; BLI, ß-lactamase inhibitor; Broad-spectrum competitive inhibitors; Crystal structure; DBO, diazabicyclooctane; ES, extended-spectrum; Halisulfates; MES, 2-(N-morpholino) ethanesulfonic acid; Marine natural products; Ni-NTA, nickel-nitrilotriacetic acid; PBP, penicillin-binding protein; R2 loop

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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Idioma: En Revista: Comput Struct Biotechnol J Ano de publicação: 2021 Tipo de documento: Article

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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Idioma: En Revista: Comput Struct Biotechnol J Ano de publicação: 2021 Tipo de documento: Article