Linked Life Data

12927533

Source:http://linkedlifedata.com/resource/pubmed/id/12927533

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2003-8-20
pubmed:abstractText
Tandem calponin-homology (CH) domains play an important role in the actin-binding function of many spectrin superfamily proteins. Crystal structures from several of these proteins have suggested a flexibility between these domains, and the manner in which these domains bind to F-actin has been the subject of some controversy. A recent paper has used electron microscopy and three-dimensional reconstruction to examine the complex of the utrophin tandem CH domain with F-actin. In contrast to our previously published study, a closed conformation of the two calponin-homology domains was suggested in the new work. We show here that the new results can be explained by incomplete binding of utrophin to actin, heterogeneity in the mode of binding, and angular disorder in F-actin. We conclude that helical averaging applied to disordered filaments is responsible for their results, and that approaches designed to separate out homogeneous subsets within such filamentous complexes offer many advantages.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0022-2836
pubmed:author
pubmed:issnType
Print
pubmed:day
29
pubmed:volume
331
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
967-72
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
Do the utrophin tandem calponin homology domains bind F-actin in a compact or extended conformation?
pubmed:affiliation
Department of Biochemistry and Molecular Genetics, University of Virginia Health Sciences Center, Jordan Hill Box 800773, Charlottesville, VA 22908-0733, USA.
pubmed:publicationType
Journal Article, In Vitro, Research Support, U.S. Gov't, P.H.S.