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Title:	Crystal Structure of Neocarzinostatin, an Antitumor Protein-Chromophore Complex
Author:	Rees, Douglas; Kim, Kyoung-Hee; Kwon, Byoung-Mog; Myers, Andrew Note: Order does not necessarily reflect citation order of authors.
Citation:	Kim, Kyoung-Hee, Byoung-Mog Kwon, Andrew G. Myers, and Douglas Rees. 1993. Crystal Structure of Neocarzinostatin, an Antitumor Protein-Chromophore Complex. Science 262(5136): 1042-1046
Access Status:	At the direction of the depositing author this work is not currently accessible through DASH.
Full Text & Related Files:	myers36.pdf (3.047Mb; PDF)
Abstract:	Structures 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.
Published Version:	http://dx.doi.org/10.1126/science.8235619
Other Sources:	http://www.chem.harvard.edu/groups/myers/publications.htm
Citable link to this page:	http://nrs.harvard.edu/urn-3:HUL.InstRepos:3119445

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  Peer reviewed scholarly articles from the Faculty of Arts and Sciences of Harvard University

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