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Synthetic antibodies for specific recognition and crystallization of structured RNA.


ABSTRACT: Antibodies that bind protein antigens are indispensable in biochemical research and modern medicine. However, knowledge of RNA-binding antibodies and their application in the ever-growing RNA field is lacking. Here we have developed a robust approach using a synthetic phage-display library to select specific antigen-binding fragments (Fabs) targeting a large functional RNA. We have solved the crystal structure of the first Fab-RNA complex at 1.95 A. Capability in phasing and crystal contact formation suggests that the Fab provides a potentially valuable crystal chaperone for RNA. The crystal structure reveals that the Fab achieves specific RNA binding on a shallow surface with complementarity-determining region (CDR) sequence diversity, length variability, and main-chain conformational plasticity. The Fab-RNA interface also differs significantly from Fab-protein interfaces in amino acid composition and light-chain participation. These findings yield valuable insights for engineering of Fabs as RNA-binding modules and facilitate further development of Fabs as possible therapeutic drugs and biochemical tools to explore RNA biology.

SUBMITTER: Ye JD 

PROVIDER: S-EPMC2224236 | biostudies-literature | 2008 Jan

REPOSITORIES: biostudies-literature

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Synthetic antibodies for specific recognition and crystallization of structured RNA.

Ye Jing-Dong JD   Tereshko Valentina V   Frederiksen John K JK   Koide Akiko A   Fellouse Frederic A FA   Sidhu Sachdev S SS   Koide Shohei S   Kossiakoff Anthony A AA   Piccirilli Joseph A JA  

Proceedings of the National Academy of Sciences of the United States of America 20071227 1


Antibodies that bind protein antigens are indispensable in biochemical research and modern medicine. However, knowledge of RNA-binding antibodies and their application in the ever-growing RNA field is lacking. Here we have developed a robust approach using a synthetic phage-display library to select specific antigen-binding fragments (Fabs) targeting a large functional RNA. We have solved the crystal structure of the first Fab-RNA complex at 1.95 A. Capability in phasing and crystal contact form  ...[more]

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