Association studies of erythoid α‐spectrin at the tetramerization site

Summary The functional roles of residues 21–43 and 55–59 in the α‐spectrin N‐terminal region in forming tetramers were determined by the introduction of mutations at each of these positions. We measured association affinities for tetramer formation (Kd), which can be used to predict clinical severit...

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Bibliographic Details
Published in:British journal of haematology 2009-11, Vol.147 (3), p.392-395
Main Authors: Lam, Vinh Q., Antoniou, Chloe, Rolius, Ramunas, Fung, Leslie W.‐M.
Format: Article
Language:English
Subjects:
Anemias. Hemoglobinopathies
Biological and medical sciences
Diseases of red blood cells
Hematologic and hematopoietic diseases
hereditary elliptocytosis
hereditary pyropoikilocytosis
Medical sciences
protein‐protein interactions
spectrin
tetramer
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Summary:Summary The functional roles of residues 21–43 and 55–59 in the α‐spectrin N‐terminal region in forming tetramers were determined by the introduction of mutations at each of these positions. We measured association affinities for tetramer formation (Kd), which can be used to predict clinical severity, of these mutants. A total of nine residues critical for association with β‐spectrin were found. The mutations of six of these residues have already been known to cause hereditary elliptocytosis or hereditary pyropoikilocytosis. Clinical symptoms associated with three mutations of residues 23, 57 and 58 have not yet been reported. We suggest that these mutations may also introduce abnormalities to erythrocytes.
ISSN:0007-1048
1365-2141
DOI:10.1111/j.1365-2141.2009.07876.x