Linked Life Data

18211803

Source:http://linkedlifedata.com/resource/pubmed/id/18211803

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2008-3-21
pubmed:abstractText
It has been known that the phosphorylation of the regulatory light chain, residing at the head/rod junction of the molecule activates the motor activity of smooth muscle and non-muscle conventional myosin (myosin II), and triggers a large conformational change of the molecule from the inhibited folded conformation to the active extended conformation. Recent structural analysis has revealed the structural basis of the inhibition of the motor function of the two heads in the inhibited conformation. On the other hand, recent studies have revealed that a processive unconventional myosin, myosin V, also shows a large change in the conformation from the folded to an extended form and this explains the activation mechanism of myosin V motor activity. These findings suggest the presence of a common scenario for the regulation of motor protein functions.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1090-2104
pubmed:author
pubmed:issnType
Electronic
pubmed:day
25
pubmed:volume
369
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
157-64
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Regulation of the function of mammalian myosin and its conformational change.
pubmed:affiliation
Department of Physiology, University of Massachusetts Medical School, 55 Lake Avenue North, Worcester, MA 01655, USA.
pubmed:publicationType
Journal Article, Review, Research Support, N.I.H., Extramural