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'''CRYSTAL STRUCTURE OF HRAS(G12V)- ANTI-RAS FV (DISULFIDE FREE MUTANT) COMPLEX''' | '''CRYSTAL STRUCTURE OF HRAS(G12V)- ANTI-RAS FV (DISULFIDE FREE MUTANT) COMPLEX''' | ||
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[[Category: Tanaka, T.]] | [[Category: Tanaka, T.]] | ||
[[Category: Williams, R L.]] | [[Category: Williams, R L.]] | ||
[[Category: | [[Category: Antibody]] | ||
[[Category: | [[Category: Cancer therapy]] | ||
[[Category: | [[Category: Disease mutation]] | ||
[[Category: | [[Category: Golgi apparatus]] | ||
[[Category: | [[Category: Gtp-binding]] | ||
[[Category: | [[Category: Immunoglobulin domain]] | ||
[[Category: | [[Category: Intrabody]] | ||
[[Category: | [[Category: Lipoprotein]] | ||
[[Category: | [[Category: Membrane]] | ||
[[Category: | [[Category: Methylation]] | ||
[[Category: | [[Category: Nucleotide- binding]] | ||
[[Category: | [[Category: Nucleotide-binding,immune system]] | ||
[[Category: | [[Category: Oncogene]] | ||
[[Category: | [[Category: Palmitate]] | ||
[[Category: | [[Category: Prenylation]] | ||
[[Category: | [[Category: Proto-oncogene]] | ||
[[Category: | [[Category: Signal transduction]] | ||
[[Category: | [[Category: Signaling protein/immune system]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 18:48:14 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on |
Revision as of 18:48, 4 May 2008
CRYSTAL STRUCTURE OF HRAS(G12V)- ANTI-RAS FV (DISULFIDE FREE MUTANT) COMPLEX
OverviewOverview
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 StructureAbout this Structure
2VH5 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
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 Sun May 4 18:48:14 2008
Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Pages with broken file links
- Homo sapiens
- Protein complex
- Rabbitts, T H.
- Tanaka, T.
- Williams, R L.
- Antibody
- Cancer therapy
- Disease mutation
- Golgi apparatus
- Gtp-binding
- Immunoglobulin domain
- Intrabody
- Lipoprotein
- Membrane
- Methylation
- Nucleotide- binding
- Nucleotide-binding,immune system
- Oncogene
- Palmitate
- Prenylation
- Proto-oncogene
- Signal transduction
- Signaling protein/immune system