| http://purl.uniprot.org/citations/11402050 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11402050 | http://www.w3.org/2000/01/rdf-schema#comment | "Baculovirus P35 is a universal suppressor of apoptosis that stoichiometrically inhibits cellular caspases in a novel cleavage-dependent mechanism. Upon caspase cleavage at Asp-87, the 10- and 25-kDa cleavage products of P35 remain tightly associated with the inhibited caspase. Mutations in the alpha-helix of the reactive site loop preceding the cleavage site abrogate caspase inhibition and antiapoptotic activity. Substitution of Pro for Val-71, which is located in the middle of this alpha-helix, produces a protein that is cleaved at the requisite Asp-87 but does not remain bound to the caspase. This loss-of-function mutation provided the opportunity to structurally analyze the conformational changes of the P35 reactive site loop after caspase cleavage. We report here the 2.7 A resolution crystal structure of V71P-mutated P35 after cleavage by human caspase-3. The structure reveals a large movement in the carboxyl-terminal side of the reactive site loop that swings down and forms a new beta-strand that augments an existing beta-sheet. Additionally, the hydrophobic amino terminus releases and extends away from the protein core. Similar movements occur when P35 forms an inhibitory complex with human caspase-8. These findings suggest that the alpha-helix mutation may alter the sequential steps or kinetics of the conformational changes required for inhibition, thereby causing P35 loss of function."xsd:string |
| http://purl.uniprot.org/citations/11402050 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m103930200"xsd:string |
| http://purl.uniprot.org/citations/11402050 | http://purl.uniprot.org/core/author | "Fisher A.J."xsd:string |
| http://purl.uniprot.org/citations/11402050 | http://purl.uniprot.org/core/author | "Friesen P.D."xsd:string |
| http://purl.uniprot.org/citations/11402050 | http://purl.uniprot.org/core/author | "dela Cruz W.P."xsd:string |
| http://purl.uniprot.org/citations/11402050 | http://purl.uniprot.org/core/date | "2001"xsd:gYear |
| http://purl.uniprot.org/citations/11402050 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/11402050 | http://purl.uniprot.org/core/pages | "32933-32939"xsd:string |
| http://purl.uniprot.org/citations/11402050 | http://purl.uniprot.org/core/title | "Crystal structure of baculovirus P35 reveals a novel conformational change in the reactive site loop after caspase cleavage."xsd:string |
| http://purl.uniprot.org/citations/11402050 | http://purl.uniprot.org/core/volume | "276"xsd:string |
| http://purl.uniprot.org/citations/11402050 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/11402050 |
| http://purl.uniprot.org/citations/11402050 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/11402050 |
| http://purl.uniprot.org/uniprot/#_P08160-mappedCitation-11402050 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/11402050 |
| http://purl.uniprot.org/uniprot/P08160 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/11402050 |