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The X‐ray Structure of the Adduct between NAMI‐A and Carbonic Anhydrase Provides Insights into the Reactivity of this Metallodrug with Proteins
Author(s) -
Casini Angela,
Temperini Claudia,
Gabbiani Chiara,
Supuran Claudiu T.,
Messori Luigi
Publication year - 2010
Publication title -
chemmedchem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.817
H-Index - 100
eISSN - 1860-7187
pISSN - 1860-7179
DOI - 10.1002/cmdc.201000331
Subject(s) - reactivity (psychology) , carbonic anhydrase , adduct , chemistry , computational biology , combinatorial chemistry , characterization (materials science) , stereochemistry , biochemistry , enzyme , organic chemistry , nanotechnology , biology , medicine , materials science , alternative medicine , pathology
Heavy metals rock! The reactivity of the antimetastatic metallodrug NAMI‐A with human carbonic anhydrase II (hCAII) has been investigated using a number of techniques, including X‐ray crystallography. The characterization of the interactions between NAMI‐A and hCAII provides valuable information on the molecular mechanisms responsible for the activity of this promising anticancer agent.