Mutation of a highly conserved isoleucine disrupts hydrophobic interactions in the alpha beta spectrin self-association binding site. [electronic resource]
- Laboratory investigation; a journal of technical methods and pathology Feb 2004
- 229-34 p. digital
Publication Type: Case Reports; Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.
0023-6837
10.1038/labinvest.3700029 doi
Binding Sites DNA Primers--chemistry Elliptocytosis, Hereditary--genetics Erythrocyte Membrane--metabolism Female Heterozygote Humans Hydrophobic and Hydrophilic Interactions Hyperbilirubinemia Infant, Newborn Isoleucine--blood Male Models, Molecular Pedigree Point Mutation Protein Conformation Sequence Analysis, DNA Spectrin--chemistry Threonine--genetics