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Abstract
A large number of proteins contain bound zinc ions. These zinc ions are frequently
coordinated by a combination of histidine and cysteine residues. In addition to atoms
that coordinate directly to the zinc ions, these side chains have groups that can
donate or accept hydrogen bonds from other groups. These secondary interactions can
help stabilize the zinc-binding sites, can contribute to protein folding and stability,
and, on occasion, can participate in interactions with other macromolecules. Five
examples of these secondary interactions are discussed: carbonic anhydrase (where
secondary interactions involving histidine residues stabilize the zinc-binding site
thermodynamically and kinetically), retroviral nucleocapsid proteins and TRAF proteins
(where cysteinate sulfur to peptide NH hydrogen bonds contribute to the structural
relationships between adjacent domains), and nucleic acid binding proteins, Zif268
and TIS11 where secondary interactions participate in protein-nucleic acid interactions.