2vh5: Difference between revisions

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[[Image:2vh5.jpg|left|200px]]
{{Seed}}
[[Image:2vh5.png|left|200px]]


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{{STRUCTURE_2vh5|  PDB=2vh5  |  SCENE=  }}  
{{STRUCTURE_2vh5|  PDB=2vh5  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF HRAS(G12V)- ANTI-RAS FV (DISULFIDE FREE MUTANT) COMPLEX'''
===CRYSTAL STRUCTURE OF HRAS(G12V)- ANTI-RAS FV (DISULFIDE FREE MUTANT) COMPLEX===




==Overview==
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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.
The line below this paragraph, {{ABSTRACT_PUBMED_18187153}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 18187153 is the PubMed ID number.
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{{ABSTRACT_PUBMED_18187153}}


==About this Structure==
==About this Structure==
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==Reference==
==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:[http://www.ncbi.nlm.nih.gov/pubmed/18187153 18187153]
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:[http://www.ncbi.nlm.nih.gov/pubmed/18187153 18187153]
Tumour prevention by a single antibody domain targeting the interaction of signal transduction proteins with RAS., Tanaka T, Williams RL, Rabbitts TH, EMBO J. 2007 Jul 11;26(13):3250-9. Epub 2007 Jun 14. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17568777 17568777]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Signal transduction]]
[[Category: Signal transduction]]
[[Category: Signaling protein/immune system]]
[[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 Tue Jul 29 14:28:42 2008''

Revision as of 11:28, 29 July 2008

File:2vh5.png

Template:STRUCTURE 2vh5

CRYSTAL STRUCTURE OF HRAS(G12V)- ANTI-RAS FV (DISULFIDE FREE MUTANT) COMPLEX

Template:ABSTRACT PUBMED 18187153

About this Structure

2VH5 is a Protein complex structure of sequences from Homo sapiens. 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

Tumour prevention by a single antibody domain targeting the interaction of signal transduction proteins with RAS., Tanaka T, Williams RL, Rabbitts TH, EMBO J. 2007 Jul 11;26(13):3250-9. Epub 2007 Jun 14. PMID:17568777

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