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dc.contributor.authorKim, Kyoung-Hee
dc.contributor.authorKwon, Byoung-Mog
dc.contributor.authorMyers, Andrew
dc.contributor.authorRees, Douglas
dc.date.accessioned2009-06-22T20:27:49Z
dc.date.issued1993
dc.identifier.citationKim, Kyoung-Hee, Byoung-Mog Kwon, Andrew G. Myers, and Douglas Rees. 1993. Crystal Structure of Neocarzinostatin, an Antitumor Protein-Chromophore Complex. Science 262(5136): 1042-1046en
dc.identifier.issn0036-8075en
dc.identifier.urihttp://nrs.harvard.edu/urn-3:HUL.InstRepos:3119445
dc.description.abstractStructures of the protein-chromophore complex and the apoprotein form of neocarzinostatin were determined at 1.8 angstrom resolution. Neocarzinostatin is composed of a labile chromophore with DNA-cleaving activity and a stabilizing protein. The chromophore displays marked nonlinearity of the triple bonds and is bound noncovalently in a pocket formed by the two protein domains. The chromophore pi-face interacts with the phenyl ring edges of Phe^52 and Phe^78. The amino sugar and carbonate groups of the chromophore are solvent exposed, whereas the epoxide, acetylene groups, and carbon C-12, the site of nucleophilic thiol addition during chromophore activation, are unexposed. The position of the amino group of the chromophore carbohydrate relative to C-12 supports the idea that the amino group plays a role in thiol activation.en
dc.description.sponsorshipChemistry and Chemical Biologyen
dc.language.isoen_USen
dc.publisherAmerican Association for the Advancement of Scienceen
dc.relation.isversionofhttp://dx.doi.org/10.1126/science.8235619en
dc.relation.hasversionhttp://www.chem.harvard.edu/groups/myers/publications.htmen
dash.licenseMETA_ONLY
dc.subjectprotein-chromophoreen
dc.subjectneocarzinostatinen
dc.subjectcrystal structureen
dc.subjectantitumoren
dc.titleCrystal Structure of Neocarzinostatin, an Antitumor Protein-Chromophore Complexen
dc.typeJournal Article
dc.description.versionVersion of Record
dc.relation.journalScienceen
dash.depositing.authorMyers, Andrew
dash.embargo.until10000-01-01
dc.identifier.doi10.1126/science.8235619*
dash.contributor.affiliatedMyers, Andrew


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