Linked Life Data

18187153

Source:http://linkedlifedata.com/resource/pubmed/id/18187153

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2008-2-5
pubmed:databankReference
pubmed:abstractText
Intracellular antibody fragments that interfere with molecular interactions inside cells are valuable in investigation of interactomes and in therapeutics, but their application demands that they function in the reducing cellular milieu. We show here a 2.7-A crystal structure of intracellular antibody folds based on scaffolds developed from intracellular antibody capture technology, and we reveal that there is no structural or functional difference with or without the intra-domain disulfide bond of the variable domain of heavy chain or the variable domain of light chain. The data indicate that, in the reducing in vivo environment, the absence of the intra-domain disulfide bond is not an impediment to correction of antibody folding or to interaction with antigen. Thus, the structural constraints for in-cell function are intrinsic to variable single-domain framework sequences, providing a generic scaffold for isolation of functional intracellular antibody single domains.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
1089-8638
pubmed:author
pubmed:issnType
Electronic
pubmed:day
22
pubmed:volume
376
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
749-57
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Functional intracellular antibody fragments do not require invariant intra-domain disulfide bonds.
pubmed:affiliation
MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't