Ontology highlight
ABSTRACT:
SUBMITTER: Boriack-Sjodin PA
PROVIDER: S-EPMC2143894 | biostudies-other | 1998 Dec
REPOSITORIES: biostudies-other
Boriack-Sjodin P A PA Zeitlin S S Chen H H HH Crenshaw L L Gross S S Dantanarayana A A Delgado P P May J A JA Dean T T Christianson D W DW
Protein science : a publication of the Protein Society 19981201 12
X-ray crystal structures of carbonic anhydrase II (CAII) complexed with sulfonamide inhibitors illuminate the structural determinants of high affinity binding in the nanomolar regime. The primary binding interaction is the coordination of a primary sulfonamide group to the active site zinc ion. Secondary interactions fine-tune tight binding in regions of the active site cavity >5 A away from zinc, and this work highlights three such features: (1) advantageous conformational restraints of a bicyc ...[more]