Linked Life Data

11072229

Source:http://linkedlifedata.com/resource/pubmed/id/11072229

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2001-2-2
pubmed:abstractText
The calcium-regulatory protein calmodulin (CaM) can bind with high affinity to a region in the cytoplasmic C-terminal tail of glycoprotein 41 of simian immunodeficiency virus (SIV). The amino acid sequence of this region is (1)DLWETLRRGGRW(13)ILAIPRRIRQGLELT(28)L. In this work, we have used near- and far-uv CD, and fluorescence spectroscopy, to study the orientation of this peptide with respect to CaM. We have also studied biosynthetically carbon-13 methyl-Met calmodulin by (1)H, (13)C heteronuclear multiple quantum coherence NMR spectroscopy. Two Trp-substituted peptides, SIV-W3F and SIV-W12F, were utilized in addition to the intact SIV peptide. Two half-peptides, SIV-N (residues 1-13) and SIV-C (residues 13-28) were also synthesized and studied. The spectroscopic results obtained with the SIV-W3F and SIV-W12F peptides were generally consistent with those obtained for the native SIV peptide. Like the native peptide, these two analogues bind with an alpha-helical structure as shown by CD spectroscopy. Fluorescence intermolecular quenching studies suggested binding of Trp3 to the C-lobe of CaM. Our NMR results show that SIV-N can bind to both lobes of calcium-CaM, and that it strongly favors binding to the C-terminal hydrophobic region of CaM. The SIV-C peptide binds with relatively low affinity to both halves of the protein. These data reveal that the intact SIV peptide binds with its N-terminal region to the carboxy-terminal region of CaM, and this interaction initiates the binding of the peptide. This orientation is similar to that of most other CaM-binding domains.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0006-3525
pubmed:author
pubmed:copyrightInfo
Copyright 2000 John Wiley & Sons, Inc.
pubmed:issnType
Print
pubmed:volume
58
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
50-62
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:11072229-Amino Acid Sequence, pubmed-meshheading:11072229-Animals, pubmed-meshheading:11072229-Binding Sites, pubmed-meshheading:11072229-Calmodulin, pubmed-meshheading:11072229-Circular Dichroism, pubmed-meshheading:11072229-HIV, pubmed-meshheading:11072229-HIV Envelope Protein gp41, pubmed-meshheading:11072229-Haplorhini, pubmed-meshheading:11072229-Humans, pubmed-meshheading:11072229-Membrane Glycoproteins, pubmed-meshheading:11072229-Molecular Sequence Data, pubmed-meshheading:11072229-Nuclear Magnetic Resonance, Biomolecular, pubmed-meshheading:11072229-Peptide Fragments, pubmed-meshheading:11072229-Protein Conformation, pubmed-meshheading:11072229-Retroviridae Proteins, pubmed-meshheading:11072229-Simian immunodeficiency virus, pubmed-meshheading:11072229-Spectrometry, Fluorescence
pubmed:year
2001
pubmed:articleTitle
Calmodulin binding properties of peptide analogues and fragments of the calmodulin-binding domain of simian immunodeficiency virus transmembrane glycoprotein 41.
pubmed:affiliation
Department of Biological Sciences, University of Calgary, Calgary, Alberta, T2N 1N4, Canada.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't