|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
2
|
|
pubmed:dateCreated |
1997-2-6
|
|
pubmed:abstractText |
The three-dimensional structure of a complex of cinnamycin, a 19-amino acid residue immunopotentiator peptide, and lysophosphatidylethanolamine was determined by 1H-NMR. The complex was cylindrical in shape, 11 A in diameter and 26 A in length, excluding the acyl chain of the phospholipid. The peptide had a hydrophobic pocket surrounded by residues Phe-7 through Ala(S)-14 to bind to the head group of the ligand. Fitting of the head group to the hydrophobic pocket was so good that other than a glycerophosphoethanolamine head group would be unable to fit the pocket. The goodness of the fitting is compatible with the strict specificity of ligand binding of the peptide.
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Feb
|
|
pubmed:issn |
0021-924X
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:volume |
119
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
226-30
|
|
pubmed:dateRevised |
2007-12-19
|
|
pubmed:meshHeading |
|
|
pubmed:year |
1996
|
|
pubmed:articleTitle |
Structure determination of an immunopotentiator peptide, cinnamycin, complexed with lysophosphatidylethanolamine by 1H-NMR1.
|
|
pubmed:affiliation |
Department of Biochemical Sciences, Gunma University.
|
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|
