| Título: | Crystal Structure of Neocarzinostatin, an Antitumor Protein-Chromophore Complex |
| Autores: |
Rees, Douglas Kim, Kyoung-Hee Kwon, Byoung-Mog Myers, Andrew |
| Fecha: |
2009-06-22 1993 |
| Publicador: | American Association for the Advancement of Science |
| Fuente: |
Ver documento |
| Tipo: | Journal Article |
| Tema: |
protein-chromophore neocarzinostatin crystal structure antitumor |
| Descripción: |
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. Chemistry and Chemical Biology |
| Idioma: | Inglés |
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