Mutation of a highly conserved isoleucine disrupts hydrophobic interactions in the αβ spectrin self-association binding site

Laboratory Investigation

Volumn 84, Issue 2, 2004, Pages 229-234

  Gallagher, Patrick G ^a,b   Zhang, Zhushan ^a   Morrow, Jon S ^a   Forget, Bernard G ^b  

^a Department of Pediatrics ^*

^b YALE UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Dynamic molecular modeling; Elliptocytosis; Mutation; Pyropoikilocytosis; Spectrin

Indexed keywords

FODRIN; ISOLEUCINE; THREONINE; PRIMER DNA; SPECTRIN;

ALLELE; ARTICLE; BINDING SITE; DROSOPHILA; ELLIPTOCYTOSIS; GENE MUTATION; GENETIC CONSERVATION; HETEROZYGOTE; HUMAN; HYDROPHILICITY; HYDROPHOBICITY; INFANT; MALE; MOLECULAR MODEL; NEWBORN HEMOLYTIC DISEASE; NEWBORN JAUNDICE; PRIORITY JOURNAL; BLOOD; CASE REPORT; CHEMICAL STRUCTURE; CHEMISTRY; DNA SEQUENCE; ERYTHROCYTE MEMBRANE; FEMALE; GENETICS; HYPERBILIRUBINEMIA; METABOLISM; NEWBORN; PEDIGREE; POINT MUTATION; PROTEIN CONFORMATION;

BINDING SITES; DNA PRIMERS; ELLIPTOCYTOSIS, HEREDITARY; ERYTHROCYTE MEMBRANE; FEMALE; HETEROZYGOTE; HUMANS; HYDROPHOBICITY; HYPERBILIRUBINEMIA; INFANT, NEWBORN; ISOLEUCINE; MALE; MODELS, MOLECULAR; PEDIGREE; POINT MUTATION; PROTEIN CONFORMATION; SEQUENCE ANALYSIS, DNA; SPECTRIN; THREONINE;

EID: 1542399545     PISSN: 00236837     EISSN: 15300307     Source Type: Journal    
DOI: 10.1038/labinvest.3700029     Document Type: Article

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