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• W2894944437 abstract "BACKGROUND Partial D status is a major concern for transfusion and pregnancy, due to the possibility of carriers becoming immunized. When known carriers of a D variant have never been exposed to complete D, they are assumed to have D partial status based on the position of the amino acid substituted. New approaches for predicting immunization risk are required. We built a three‐dimensional (3D) structural model to investigate the consequences of substitutions of Amino Acid 223 involved in a large number of D variants. STUDY DESIGN AND METHODS Homology modeling was performed with multiple templates. The model was evaluated by comparing the interactions of the known p.Phe223Val variant ( RHD*08.01 ) and a new p.Phe223Ser variant ( RHD*52) to RhD reference allele (p.Phe223). The consequences predicted by modeling the variants were compared with serologic data. RESULTS The 3D structural model was generated from two related protein structures and assessed with state‐of‐the‐art approaches. An analysis of the interactions of the variant Residue 223 in the proposed 3D model highlighted the importance of this position. Modeling predictions were consistent with the serologic and clinical data obtained for the D antigen with a substitution of Amino Acid 223. CONCLUSION We used a 3D structural model to evaluate the effect of the p.Phe223 substitution on the conformation of the RhD protein. This model shed light on the influence of substitutions on the structure of the RhD protein and the associated alloimmunization risk. These initial findings indicate that the p.Phe223Ser variant can be considered partial." @default.
• W2894944437 created "2018-10-12" @default.
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• W2894944437 date "2018-10-04" @default.
• W2894944437 modified "2023-10-17" @default.
• W2894944437 title "Alloimmunization risk associated with amino acid 223 substitution in the RhD protein: analysis in the light of molecular modeling" @default.
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• W2894944437 doi "https://doi.org/10.1111/trf.14809" @default.
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