|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
10
|
|
pubmed:dateCreated |
2009-5-4
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|
pubmed:abstractText |
C-terminal-lacking fragments of the anti-mycobacterial peptide lariatin A were obtained by hydrolysis using carboxypeptidase P and their anti-mycobacterial activities were evaluated. Lys17 was found to be essential for their antimicrobial activity. A molecular dynamics simulation, with explicit water molecules, helped determine the structural characteristics of Lys17 of lariatin A. The simulation revealed the dynamic formation and deformation of a salt bridge between the N(xi) atom of Lys17 and the carboxyl group of C-terminal Pro18, which is deemed to be crucial for the compound's anti-mycobacterial activity.
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|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
May
|
|
pubmed:issn |
1464-3405
|
|
pubmed:author |
|
|
pubmed:issnType |
Electronic
|
|
pubmed:day |
15
|
|
pubmed:volume |
19
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
2888-90
|
|
pubmed:meshHeading |
|
|
pubmed:year |
2009
|
|
pubmed:articleTitle |
Lys17 in the 'lasso' peptide lariatin A is responsible for anti-mycobacterial activity.
|
|
pubmed:affiliation |
Center for Basic Research, Kitasato University, Shirokane, Minato-ku, Tokyo, Japan.
|
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|
