dc.date.accessioned | 2016-06-07T13:51:03Z | |
dc.date.available | 2016-06-07T13:51:03Z | |
dc.date.created | 2016-04-18T18:42:38Z | |
dc.date.issued | 2016 | |
dc.identifier.citation | Cordara, Gabriele van Eerde, André Grahn, Elin Winter, HC Goldstein, IJ Krengel, Ute . An Unusual Member of the Papain Superfamily: Mapping the Catalytic Cleft of the Marasmius oreades agglutinin (MOA) with a Caspase Inhibitor. PLoS ONE. 2016, 11(2), e0149407 | |
dc.identifier.uri | http://hdl.handle.net/10852/50438 | |
dc.description.abstract | Papain-like cysteine proteases (PLCPs) constitute the largest group of thiol-based protein degrading enzymes and are characterized by a highly conserved fold. They are found in bacteria, viruses, plants and animals and involved in a number of physiological and pathological processes, parasitic infections and host defense, making them interesting targets for drug design. The Marasmius oreades agglutinin (MOA) is a blood group B-specific fungal chimerolectin with calcium-dependent proteolytic activity. The proteolytic domain of MOA presents a unique structural arrangement, yet mimicking the main structural elements in known PLCPs. Here we present the X-ray crystal structure of MOA in complex with Z-VAD-fmk, an irreversible caspase inhibitor known to cross-react with PLCPs. The structural data allow modeling of the substrate binding geometry and mapping of the fundamental enzyme-substrate interactions. The new information consolidates MOA as a new, yet strongly atypical member of the papain superfamily. The reported complex is the first published structure of a PLCP in complex with the well characterized caspase inhibitor Z-VAD-fmk. | en_US |
dc.language | EN | |
dc.language.iso | en | en_US |
dc.publisher | Public Library of Science (PLoS) | |
dc.rights | Public Domain Dedication | |
dc.rights.uri | https://creativecommons.org/publicdomain/zero/1.0/ | |
dc.title | An Unusual Member of the Papain Superfamily: Mapping the Catalytic Cleft of the Marasmius oreades agglutinin (MOA) with a Caspase Inhibitor | en_US |
dc.type | Journal article | en_US |
dc.creator.author | Cordara, Gabriele | |
dc.creator.author | van Eerde, André | |
dc.creator.author | Grahn, Elin | |
dc.creator.author | Winter, HC | |
dc.creator.author | Goldstein, IJ | |
dc.creator.author | Krengel, Ute | |
cristin.unitcode | 185,15,12,0 | |
cristin.unitname | Kjemisk institutt | |
cristin.ispublished | true | |
cristin.fulltext | original | |
cristin.qualitycode | 1 | |
dc.identifier.cristin | 1351084 | |
dc.identifier.bibliographiccitation | info:ofi/fmt:kev:mtx:ctx&ctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=PLoS ONE&rft.volume=11&rft.spage=e0149407&rft.date=2016 | |
dc.identifier.jtitle | PLoS ONE | |
dc.identifier.volume | 11 | |
dc.identifier.issue | 2 | |
dc.identifier.doi | http://dx.doi.org/10.1371/journal.pone.0149407 | |
dc.identifier.urn | URN:NBN:no-54030 | |
dc.type.document | Tidsskriftartikkel | en_US |
dc.type.peerreviewed | Peer reviewed | |
dc.source.issn | 1932-6203 | |
dc.identifier.fulltext | Fulltext https://www.duo.uio.no/bitstream/handle/10852/50438/1/journal.pone.0149407.pdf | |
dc.type.version | PublishedVersion | |
cristin.articleid | e0149407 | |