Structural basis for specific inhibition of Autotaxin by a DNA aptamer View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2016-05

AUTHORS

Kazuki Kato, Hisako Ikeda, Shin Miyakawa, Satoshi Futakawa, Yosuke Nonaka, Masatoshi Fujiwara, Shinichi Okudaira, Kuniyuki Kano, Junken Aoki, Junko Morita, Ryuichiro Ishitani, Hiroshi Nishimasu, Yoshikazu Nakamura, Osamu Nureki

ABSTRACT

ATX is a plasma lysophospholipase D that hydrolyzes lysophosphatidylcholine (LPC) and produces lysophosphatidic acid. To date, no ATX-inhibition-mediated treatment strategies for human diseases have been established. Here, we report anti-ATX DNA aptamers that inhibit ATX with high specificity and efficacy. We solved the crystal structure of ATX in complex with the anti-ATX aptamer RB011, at 2.0-Å resolution. RB011 binds in the vicinity of the active site through base-specific interactions, thus preventing the access of the choline moiety of LPC substrates. Using the structural information, we developed the modified anti-ATX DNA aptamer RB014, which exhibited in vivo efficacy in a bleomycin-induced pulmonary fibrosis mouse model. Our findings reveal the structural basis for the specific inhibition of ATX by the anti-ATX aptamer and highlight the therapeutic potential of anti-ATX aptamers for the treatment of human diseases, such as pulmonary fibrosis. More... »

PAGES

395-401

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nsmb.3200

DOI

http://dx.doi.org/10.1038/nsmb.3200

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1030350634

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/27043297


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