Linked Life Data

10380228

Source:http://linkedlifedata.com/resource/pubmed/id/10380228

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1999-8-10
pubmed:abstractText
Recombinant forms of the N-terminal domain of the cell adhesion receptor CD2 adopt a variety of olds by exchange of beta-sheets between adjacent polypeptide chains. Although these interdigitated forms are normally metastable, we have used site-directed mutagenesis to alter the kinetics of formation and relative stabilities of these states, leading to spontaneous formation of monomeric, dimeric, trimeric and tetrameric intertwined folded states. A characteristic feature of these fold-disorder-alternative fold transitions is the independence of each domain folding event, as deduced from kinetic analysis of folding data. Structures for fully interdigitated trimeric and tetrameric forms have been modelled, consistent with both the crystallographic and kinetic data. Although the biological role of these alternative folded states remains unclear, these structures form a remarkable demonstration of the fluidity of structure generated from a single polypeptide chain.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1793-5091
pubmed:author
pubmed:issnType
Print
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
566-77
pubmed:dateRevised
2007-9-12
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
One sequence, four folds: transitions between an ensemble of metastable folds for the N-terminal domain of CD2.
pubmed:affiliation
Department of Biochemistry, University of Bristol, U.K.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't