Linked Life Data

8340411

Source:http://linkedlifedata.com/resource/pubmed/id/8340411

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
21
pubmed:dateCreated
1993-8-30
pubmed:abstractText
FN-C/H II (KNNQKSEPLIGRKKT), a heparin-binding peptide derived from the COOH-terminal heparin-binding domain of fibronectin, mediates cell adhesion for a variety of cell types and promotes neurite outgrowth. By systematic amino acid substitution of synthetic peptide analogues of FN-C/H II, the basic structural features necessary for activity have been identified in the COOH-terminal residues LIGRKK. This biologically "active" sequence has been located in several other heparin/heparan sulfate-binding proteins and may represent a potential binding motif for sulfated polyanions. NMR structural studies indicate that the COOH-terminal segment of FN-C/H II displays significant multiple-turn or helix-like character suggesting that the RKK sequence may lie on the same surface of the protein, as opposed to alternating in an extended chain motif.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
268
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
15859-67
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Structural features of fibronectin synthetic peptide FN-C/H II, responsible for cell adhesion, neurite extension, and heparan sulfate binding.
pubmed:affiliation
Department of Laboratory Medicine, University of Minnesota, Minneapolis 55455.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't