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Article

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

Blood - 10 Jun 2010

Ipsaro Jonathan J, Harper Sandra L, Messick Troy E, Marmorstein Ronen, Mondragón Alfonso, Speicher David W

Abstract excerpt

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. Alth...

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Topics

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Share to Crystallography, X-Ray
Share to Elliptocytosis, Hereditary
Share to Erythrocyte Membrane

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutagenesis, Site-Directed

Share to Protein Multimerization

Share to Protein Structure, Quaternary

Share to Spectrin

Share to Structure-Activity Relationship

Source

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Identifiers

PMID: 20197550
DOI: 10.1182/blood-2010-01-261396
PMCID: PMC2890174

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-20197550-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

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