Linked Life Data

14527664

Source:http://linkedlifedata.com/resource/pubmed/id/14527664

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2-3
pubmed:dateCreated
2003-10-6
pubmed:abstractText
Gelsolin requires activation to carry out its severing and capping activities on F-actin. Here, we present the structure of the isolated C-terminal half of gelsolin (G4-G6) at 2.0 A resolution in the presence of Ca(2+) ions. This structure completes a triptych of the states of activation of G4-G6 that illuminates its role in the function of gelsolin. Activated G4-G6 displays an open conformation, with the actin-binding site on G4 fully exposed and all three type-2 Ca(2+) sites occupied. Neither actin nor the type-l Ca(2+), which normally is sandwiched between actin and G4, is required to achieve this conformation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
552
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
82-5
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
Activation in isolation: exposure of the actin-binding site in the C-terminal half of gelsolin does not require actin.
pubmed:affiliation
Department of Medical Biochemistry and Microbiology, Uppsala University, Box 582, 751 23 Uppsala, Sweden.
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't