Linked Life Data

6894930

Source:http://linkedlifedata.com/resource/pubmed/id/6894930

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1981-10-25
pubmed:abstractText
Rotary-shadowed filamin molecules appear as long, highly flexible rods curved into a variety of configurations. The particles observed were 2.7 nm wide but had contour lengths of either 98 nm or 193 nm. The longer particles are probably end-to-end dimers of the shorter but it is not clear how many polypeptide chains these particles contain. Heavy merofilamin, obtained by digestion of filamin with a calcium-activated protease from muscle, has been used to investigate where filamin binds on the actin filaments. Negatively stained filaments of actin plus heavy merofilamin resemble those of pure actin; occasionally rod-shaped material sticking out from the filament is observed suggesting that the elongated shape of filamin is maintained after digestion. Optical diffraction patterns of electron micrographs of paracrystals of actin plus heavy merofilamin indicate that the helical symmetry of the actin filament is unchanged, but the observed interfilament spacing is larger than in F-actin paracrystals. Increased intensity of the second layer-line reflection is observed, suggesting that additional material is lying along the grooves of the actin helix. The elongated shape of filamin and its ability to bind to F-actin in a way similar to tropomyosin suggest a possible role for this protein in regulating the organization and aggregation of actin filaments.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0142-4319
pubmed:author
pubmed:issnType
Print
pubmed:volume
2
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
193-202
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1981
pubmed:articleTitle
Structure of filamin and the F-actin-heavy merofilamin complex.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't