Linked Life Data

8307157

Source:http://linkedlifedata.com/resource/pubmed/id/8307157

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1994-3-11
pubmed:abstractText
The F-actin binding properties of chicken villin, its headpiece and domains 2-3 (V2-3) have been analysed to identify sites involved in bundle formation. Headpiece and V2-3 bind actin with Kd values of approximately 7 microM and approximately 0.3 microM, respectively, at low ionic strength. V2-3 binding, like that of villin, is weakened with increasing salt concentration; headpiece binding is not. Competition experiments show that headpiece and V2-3 bind to different sites on actin, forming the two cross-linking sites of villin. Headpiece does not compete with the F-actin binding domains of gelsolin or alpha-actinin, but it dissociates actin depolymerizing factor. We suggest that the F-actin binding domains of actin severing, crosslinking and capping proteins can be organized into two classes.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
24
pubmed:volume
338
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
58-62
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Characterisation of the F-actin binding domains of villin: classification of F-actin binding proteins into two groups according to their binding sites on actin.
pubmed:affiliation
MRC Laboratory of Molecular Biology, Cambridge, UK.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.