Linked Life Data

12492898

Source:http://linkedlifedata.com/resource/pubmed/id/12492898

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2002-12-20
pubmed:abstractText
Recently, it has been shown that mammalian PEBPs are implicated in several signalling pathways controlling the cellular cycle. In particular, during brain development, the N-terminal part of mammalian PEBP is specifically cleaved and the resulting 11 amino acid peptide stimulates the growth and activity of acetylcholinergic neurons. The crystallographic structure of bovine and human PEBPs has revealed that their N- and C-terminal parts are accessible and exposed to the solvent suggesting that they may be involved in specific interactions with cellular partners. We have chemically synthetized the two peptides corresponding to these terminal parts and studied their structure in solution by circular dichroism and NMR spectroscopies: both of them are well-structured. The N-terminal peptide is composed of a series of turns, leading to a hook conformation. The C-terminal peptide displays a globally helical conformation similar to that observed in the whole protein; it is characterized by an amphipatic feature with a hydrophobic cluster located on one side. These structural features enlighten previous fluorescence and monolayer experiments and give new insights on the roles of both PEBP termini.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
1397-002X
pubmed:author
pubmed:issnType
Print
pubmed:volume
61
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
47-57
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed-meshheading:12492898-Amino Acid Sequence, pubmed-meshheading:12492898-Androgen-Binding Protein, pubmed-meshheading:12492898-Animals, pubmed-meshheading:12492898-Carrier Proteins, pubmed-meshheading:12492898-Cattle, pubmed-meshheading:12492898-Circular Dichroism, pubmed-meshheading:12492898-Humans, pubmed-meshheading:12492898-Hydrophobic and Hydrophilic Interactions, pubmed-meshheading:12492898-Magnetic Resonance Spectroscopy, pubmed-meshheading:12492898-Models, Molecular, pubmed-meshheading:12492898-Molecular Sequence Data, pubmed-meshheading:12492898-Peptide Fragments, pubmed-meshheading:12492898-Phosphatidylethanolamine Binding Protein, pubmed-meshheading:12492898-Phospholipid Transfer Proteins, pubmed-meshheading:12492898-Protein Interaction Mapping, pubmed-meshheading:12492898-Sequence Homology, pubmed-meshheading:12492898-Solutions
pubmed:year
2003
pubmed:articleTitle
Peptides corresponding to the N- and C-terminal parts of PEBP are well-structured in solution: new insights into their possible interaction with partners in vivo.
pubmed:affiliation
Centre de Biophysique Moléculaire, Centre National de la Recherche Scientifique, UPR 4301, University of Orléans and INSERM, rue Charles Sadron, Orleans, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't