Linked Life Data

11305911

Source:http://linkedlifedata.com/resource/pubmed/id/11305911

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
16
pubmed:dateCreated
2001-4-18
pubmed:abstractText
Titin and alpha-actinin, two modular muscle proteins, are with actin the major components of the Z-band in vertebrate striated muscles where they serve to organize the antiparallel actin filament arrays in adjacent sarcomeres and to transmit tension between sarcomeres during activation. Interactions between titin and alpha-actinin have been mainly localized in a 45-amino acid multiple motif (Z-repeat) in the N-terminal region of titin and the C-terminal region of alpha-actinin. In this study, we provide the first quantitative characterization of alpha-actinin-Z-repeat recognition and dissect the interaction to its minimal units. Different complementary techniques, such as circular dichroism, calorimetry, and nuclear magnetic spectroscopy, were used. Two overlapping alpha-actinin constructs (Act-EF34 and Act-EF1234) containing two and four EF-hand motifs, respectively, were produced, and their folding properties were examined. Complex formation of Act-EF34 and Act-EF1234 with single- and double-Z-repeat constructs was studied. Act-EF34 was shown quantitatively to be necessary and sufficient for binding to Z-repeats, excluding the presence of additional high-affinity binding sites in the remaining part of the domain. The binding affinities of the different Z-repeats for Act-EF34 range from micromolar to millimolar values. The strongest of these interactions are comparable to those observed in troponin C-troponin I complexes. The binding affinities for Act-EF34 are maximal for Zr1 and Zr7, the two highly homologous sequences present in all muscle isoforms. No cooperative or additional contributions to the interaction were observed for Z-repeat double constructs. These findings have direct relevance for evaluating current models of Z-disk assembly.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
24
pubmed:volume
40
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4957-65
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:11305911-Actinin, pubmed-meshheading:11305911-Amino Acid Sequence, pubmed-meshheading:11305911-Animals, pubmed-meshheading:11305911-Calorimetry, pubmed-meshheading:11305911-Circular Dichroism, pubmed-meshheading:11305911-EF Hand Motifs, pubmed-meshheading:11305911-Escherichia coli, pubmed-meshheading:11305911-Humans, pubmed-meshheading:11305911-Magnetic Resonance Spectroscopy, pubmed-meshheading:11305911-Molecular Sequence Data, pubmed-meshheading:11305911-Muscle Proteins, pubmed-meshheading:11305911-Peptide Fragments, pubmed-meshheading:11305911-Protein Binding, pubmed-meshheading:11305911-Protein Folding, pubmed-meshheading:11305911-Protein Kinases, pubmed-meshheading:11305911-Protein Structure, Secondary, pubmed-meshheading:11305911-Protein Structure, Tertiary, pubmed-meshheading:11305911-Rabbits, pubmed-meshheading:11305911-Recombinant Fusion Proteins, pubmed-meshheading:11305911-Repetitive Sequences, Amino Acid, pubmed-meshheading:11305911-Structure-Activity Relationship
pubmed:year
2001
pubmed:articleTitle
A structural characterization of the interactions between titin Z-repeats and the alpha-actinin C-terminal domain.
pubmed:affiliation
NIMR, The Ridgeway, London NW7 1AA, UK.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't