Structure of the alpha beta spectrin dimer and mutations that cause hereditary elliptocytosis

This depiction of the erythrocyte spectrin tetramerization domain was created using UCSF Chimera software^[1] and based on the crystal structure^[2] deposited in protein database (PDB) as 3LBX.

α-spectrin amino acid residues – Missense mutations have been reported to cause HE^[3] or HPP when present in trans with a low-expression SPTA1 allele (most commonly α-LELY).
β-spectrin amino acid residues – Heterozygosity for a pathogenic variant causes HE. Homozygosity or compound heterozygosity for pathogenic variants causes HPP.

UCSF: University of California San Francisco; HE: hereditary elliptocytosis; HPP: hereditary pyropoikilocytosis; SPTA1: gene that encodes erythrocyte alpha-spectrin; α-LELY: alpha-spectrin low-expression allele Lyon.

Courtesy of Theodosia Kalfa, MD, PhD.

References:

Petterson EF, Goddard TD, Huang CC, et al. UCSF Chimera - a visualization system for exploratory and research analysis. J Comput Chem 2004; 25:1605.
Isparo JJ, Harper SL, Messick TE, et al. Crystal structure and functional interpretation of the erythrocyte spectrin tetramerization domain complex. Blood 2010; 115:4843.
Gaetani M, Mootien S, Harper S, et al. Structural and functional aspects of hereditary hemolytic anemia-associated point mutations in the alpha spectrin tetramer site. Blood 2008; 111:5712.

Graphic 140172 Version 1.0

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Structure of the alpha beta spectrin dimer and mutations that cause hereditary elliptocytosis