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Red cell adenylate kinase deficiency: molecular study of 3 new mutations (118G>A, 190G>A, and GAC deletion) associated with hereditary nonspherocytic hemolytic.

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Presentation on theme: "Red cell adenylate kinase deficiency: molecular study of 3 new mutations (118G>A, 190G>A, and GAC deletion) associated with hereditary nonspherocytic hemolytic."— Presentation transcript:

1 Red cell adenylate kinase deficiency: molecular study of 3 new mutations (118G>A, 190G>A, and GAC deletion) associated with hereditary nonspherocytic hemolytic anemia by Joan-Lluis Vives Corrons, Estefania Garcia, Joan J. Tusell, Kottayil I. Varughese, Carol West, and Ernest Beutler Blood Volume 102(1): July 1, 2003 ©2003 by American Society of Hematology

2 A comparison porcine and human AK
A comparison porcine and human AK. Numbers and asterisks indicate the consecutive sequence of amino acid residues: * (10, 30, 50, etc) and number (20, 40, 60, etc). A comparison porcine and human AK. Numbers and asterisks indicate the consecutive sequence of amino acid residues: * (10, 30, 50, etc) and number (20, 40, 60, etc). Gray shaded areas indicate the amino acid differences between porcine and human AK. Joan-Lluis Vives Corrons et al. Blood 2003;102: ©2003 by American Society of Hematology

3 A stereoscopic view of a model for the human AK bound to the substrate AMP. The locations of the 3 mutations, 40, 64, and 140 (141), are indicated in red. A stereoscopic view of a model for the human AK bound to the substrate AMP. The locations of the 3 mutations, 40, 64, and 140 (141), are indicated in red. The flexible loop containing residue 64 is shown in orange and AMP in blue. The N and C termini are labeled as N and C. The figure was produced using the program BOBSCRIPT.15 Joan-Lluis Vives Corrons et al. Blood 2003;102: ©2003 by American Society of Hematology


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