The structure and evolution of the murine inhibitor of carbonic anhydrase: a member of the transferrin superfamily.

ABSTRACT: The original signature of the transferrin (TF) family of proteins was the ability to bind ferric iron with high affinity in the cleft of each of two homologous lobes. However, in recent years, new family members that do not bind iron have been discovered. One new member is the inhibitor of carbonic anhydrase (ICA), which as its name indicates, binds to and strongly inhibits certain isoforms of carbonic anhydrase. Recently, mouse ICA has been expressed as a recombinant protein in a mammalian cell system. Here, we describe the 2.4 Å structure of mouse ICA from a pseudomerohedral twinned crystal. As predicted, the structure is bilobal, comprised of two α-β domains per lobe typical of the other family members. As with all but insect TFs, the structure includes the unusual reverse γ-turn in eac

SUBMITTER: Eckenroth BE 

PROVIDER: S-EPMC2975126 | biostudies-literature | 2010 Sep

REPOSITORIES: biostudies-literature