TY  - JOUR
AU  - Schäfer, Martina
AU  - Schneider, Thomas R
AU  - Sheldrick, George M
TI  - Crystal structure of vancomycin
JO  - Structure
VL  - 4
IS  - 12
SN  - 0969-2126
CY  - London [u.a.]
PB  - Elsevier Science
M1  - PUBDB-2017-06937
SP  - 1509 - 1515
PY  - 1996
N1  - F-Bereich; EMBL
AB  - 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’.
LB  - PUB:(DE-HGF)16
UR  - <Go to ISI:>//WOS:A1996VY73900012
C6  - pmid:8994975
DO  - DOI:10.1016/S0969-2126(96)00156-6
UR  - https://bib-pubdb1.desy.de/record/330445
ER  -