期刊
JOURNAL OF MOLECULAR BIOLOGY
卷 376, 期 3, 页码 749-757出版社
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2007.11.085
关键词
intrabody; RAS; single domains; X-ray crystallography; disulfide-free
资金
- Medical Research Council [MC_U105178807] Funding Source: researchfish
- MRC [MC_U105178807] Funding Source: UKRI
- Medical Research Council [MC_U105178807] Funding Source: Medline
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-angstrom 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. (C) 2007 Elsevier Ltd. All rights reserved.
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