Journal Article

PUBDB-2017-06937

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Crystal structure of vancomycin

Schäfer, M. ; Schneider, T. R. ; Sheldrick, G. M. (Corresponding author)

1996
Elsevier Science London [u.a.]

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Please use a persistent id in citations: doi:10.1016/S0969-2126(96)00156-6

Abstract: Vancomycin and other related glycopeptide antibiotics are clinically very important because they often represent the last line of defence against bacteria that have developed resistance to antibiotics. Vancomycin is believed to act by binding nascent cell wall mucopeptides terminating in the sequence Full-size image (<1 K)-Ala–Full-size image (<1 K)-Ala, weakening the resulting cell wall. Extensive NMR and other studies have shown that the formation of asymmetric antibiotic dimers is important in peptide binding. Despite intensive efforts the crystal structure of vancomycin has been extremely difficult to obtain, partly because high-resolution data were available, and partly because the structure was too large to be solved by conventional ‘direct methods’.

Note: F-Bereich; EMBL

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Contributing Institute(s):

1. DESY Retrocat (DESY(-2012))

Research Program(s):

1. 899 - ohne Topic (POF3-899) (POF3-899)

Experiment(s):

1. No specific instrument

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Database coverage:
; BIOSIS Previews ; Current Contents - Life Sciences ; Ebsco Academic Search ; NCBI Molecular Biology Database ; Nationallizenz ; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection

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