Linked Life Data

19636946

Source:http://linkedlifedata.com/resource/pubmed/id/19636946

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2009-7-28
pubmed:abstractText
Filamins are large actin-binding and cross-linking proteins which act as linkers between the cytoskeleton and various signaling proteins. Filamin A (FLNa) is the most abundant of the three filamin isoforms found in humans. FLNa contains an N-terminal actin-binding domain and 24 immunoglobulin-like (Ig) domains. The Ig domains are responsible for the FLNa dimerization and most of the interactions that FLNa has with numerous other proteins. There are several crystal and solution structures from isolated single Ig domains of filamins in the PDB database, but only few from longer constructs. Here, we present nearly complete chemical shift assignments of FLNa tandem Ig domains 16-17 and 18-19. Chemical shift mapping between FLNa tandem Ig domain 16-17 and isolated domain 17 suggests a novel domain-domain interaction mode.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
1874-270X
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
3
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
53-6
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
1H, 13C and 15N resonance assignments of the human filamin A tandem immunoglobulin-like domains 16-17 and 18-19.
pubmed:affiliation
Laboratory of Organic Chemistry, Department of Chemistry, University of Helsinki, A.I. Virtasen Aukio 1, P.O. Box 55, 00014, Helsinki, Finland. Outi.K.Heikkinen@helsinki.fi
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't