Linked Life Data

2976938

Source:http://linkedlifedata.com/resource/pubmed/id/2976938

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1989-5-11
pubmed:abstractText
A new family of proteins (annexins) that bind to membranes at micromolar free Ca2+ has been recognized. Its members include an EGF-receptor kinase substrate (p35), a retroviral tyrosine kinase substrate (p36), the liver protein endonexin (p32) and an electric ray protein, calelectrin. Each protein contains four sequence repeats with a further 2-fold internal homology. Using the predicted secondary structure and pattern of conserved hydrophobic residues in each repeat, we have built a three-dimensional model that is largely isostructural with the known molecular conformation of bovine intestinal calcium-binding protein. The final (energy-refined) model had a core formed from the conserved hydrophobic residues. It differed from ICaBP principally in the length of the two Ca2+-binding loops with only one loop being able to bind. The model suggests a mechanism for interaction of these new Ca2+-binding proteins with phospholipid bilayers.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0269-2139
pubmed:author
pubmed:issnType
Print
pubmed:volume
1
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
183-7
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
Predicted structure for the calcium-dependent membrane-binding proteins p35, p36, and p32.
pubmed:affiliation
Department of Crystallography, Birkbeck College, London, UK.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't