2vh5
From Proteopedia
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CRYSTAL STRUCTURE OF HRAS(G12V)- ANTI-RAS FV (DISULFIDE FREE MUTANT) COMPLEX
Overview
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.
About this Structure
2VH5 is a Protein complex structure of sequences from Homo sapiens with , and as ligands. Known structural/functional Sites: , and . Full crystallographic information is available from OCA.
Reference
Functional intracellular antibody fragments do not require invariant intra-domain disulfide bonds., Tanaka T, Rabbitts TH, J Mol Biol. 2008 Feb 22;376(3):749-57. Epub 2007 Dec 4. PMID:18187153
Page seeded by OCA on Thu Feb 21 18:56:10 2008
Categories: Homo sapiens | Protein complex | Rabbitts, T H. | Tanaka, T. | Williams, R L. | GTP | MG | ZN | Antibody | Cancer therapy | Disease mutation | Golgi apparatus | Gtp-binding | Immune system | Immunoglobulin domain | Intrabody | Lipoprotein | Membrane | Methylation | Nucleotide- binding | Nucleotide-binding | Oncogene | Palmitate | Prenylation | Proto-oncogene | Signal transduction | Signaling protein/immune system
