Linked Life Data

12721770

Source:http://linkedlifedata.com/resource/pubmed/id/12721770

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
2003-10-30
pubmed:abstractText
A number of DD-peptidases have been reported to interact with the membrane via C-terminal amphiphilic alpha-helices, but experimental support for this rests with a few well-characterized cases. These show the C-terminal interactions of DD-carboxypeptidases to involve high levels of membrane penetration, DD-endopeptidases to involve membrane surface binding and class C penicillin-binding proteins to involve membrane binding with intermediate properties. Here, we have characterized C-terminal alpha-helices from each of these peptidase groups according to their amphiphilicity, as measured by mean <microH>, and the corresponding mean hydrophobicity, <H>. Regression and statistical analyses showed these properties to exhibit parallel negative linear relationships, which resulted from the spatial ordering of alpha-helix amino acid residues. Taken with the results of compositional and graphical analyses, our results suggest that the use of C-terminal alpha-helices may be a universal feature of the membrane anchoring for each of these groups of DD-peptidases. Moreover, to accommodate differences between these mechanisms, each group of C-terminal alpha-helices optimizes its structural amphiphilicity and hydrophobicity to fulfil its individual membrane-anchoring function. Our results also show that each anchor type analysed requires a similar overall balance between amphiphilicity for membrane interaction, which we propose is necessary to stabilize their initial membrane associations. In addition, we present a methodology for the prediction of C-terminal alpha-helical anchors from the classes of DD-peptidases analysed, based on a parallel linear model.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0175-7571
pubmed:author
pubmed:issnType
Print
pubmed:volume
32
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
589-98
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:12721770-Amino Acid Sequence, pubmed-meshheading:12721770-Binding Sites, pubmed-meshheading:12721770-Carboxypeptidases, pubmed-meshheading:12721770-Computer Simulation, pubmed-meshheading:12721770-Databases, Protein, pubmed-meshheading:12721770-Enzyme Activation, pubmed-meshheading:12721770-Linear Models, pubmed-meshheading:12721770-Membrane Proteins, pubmed-meshheading:12721770-Models, Chemical, pubmed-meshheading:12721770-Models, Molecular, pubmed-meshheading:12721770-Models, Statistical, pubmed-meshheading:12721770-Molecular Sequence Data, pubmed-meshheading:12721770-Peptide Hydrolases, pubmed-meshheading:12721770-Protein Binding, pubmed-meshheading:12721770-Protein Conformation, pubmed-meshheading:12721770-Protein Structure, Secondary, pubmed-meshheading:12721770-Reproducibility of Results, pubmed-meshheading:12721770-Sensitivity and Specificity, pubmed-meshheading:12721770-Sequence Analysis, Protein, pubmed-meshheading:12721770-Serine-Type D-Ala-D-Ala Carboxypeptidase, pubmed-meshheading:12721770-Structure-Activity Relationship, pubmed-meshheading:12721770-Surface-Active Agents
pubmed:year
2003
pubmed:articleTitle
A statistical investigation of amphiphilic properties of C-terminally anchored peptidases.
pubmed:affiliation
Department of Physics, Astronomy and Mathematics, University of Central Lancashire, Preston, PR1 2HE, UK.
pubmed:publicationType
Journal Article, Comparative Study, Evaluation Studies