Crystal structure and functional interpretation of the erythrocyte spectrin tetramerization domain complex.

ABSTRACT: As the principal component of the membrane skeleton, spectrin confers integrity and flexibility to red cell membranes. Although this network involves many interactions, the most common hemolytic anemia mutations that disrupt erythrocyte morphology affect the spectrin tetramerization domains. Although much is known clinically about the resulting conditions (hereditary elliptocytosis and pyropoikilocytosis), the detailed structural basis for spectrin tetramerization and its disruption by hereditary anemia mutations remains elusive. Thus, to provide further insights into spectrin assembly and tetramer site mutations, a crystal structure of the spectrin tetramerization domain complex has been determined. Architecturally, this complex shows striking resemblance to multirepeat spectrin fragments

SUBMITTER: Ipsaro JJ 

PROVIDER: S-EPMC2890174 | biostudies-literature | 2010 Jun

REPOSITORIES: biostudies-literature