Linked Life Data

3625715

Source:http://linkedlifedata.com/resource/pubmed/id/3625715

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
1987-10-9
pubmed:abstractText
A series of 20 C-terminal fragment analogues of the anticoagulant peptide hirudin were synthesized by solid-phase techniques in order to investigate the nature of the thrombin-hirudin interaction. Inhibition of plasma fibrin clot formation by thrombin in vitro was used as a measure of anticoagulant activity. In the minimum region necessary for detectable anticoagulant activity, hirudin56-64, positions Phe56, Glu57, Ile59, Pro60, and Leu64 are sensitive to modification. These residues are apparently important for direct interaction with thrombin or for maintaining a favorable conformation for the interaction. On the basis of conformational analysis of this region by computational methods, a "kinked" amphipathic alpha-helical structure, which orients all of the residues most critical for activity on one face of the helix, is proposed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0022-2623
pubmed:author
pubmed:issnType
Print
pubmed:volume
30
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1688-91
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
Anticoagulant peptides: nature of the interaction of the C-terminal region of hirudin with a noncatalytic binding site on thrombin.
pubmed:publicationType
Journal Article