Biochemical and computational analyses of two phenotypically related @entity29272 mutations ( @entity73170 and @entity73171 ) that XXXX .

@entity1 @entity73169 @entity73170 @entity29272 @entity73171 @entity209 @entity1624
UNASSIGNED: @entity1624 is a @entity209 caused by mutations in the @entity29272 gene [1,2]. We encountered a @entity1 heterozygous for a known pathogenic @entity73169 mutation and a novel @entity73170 variant of unknown significance [3]. Reminiscent of @entity1 with the @entity73171 mutation, our @entity1 had loss of @entity29272 enzyme activity in erythrocytes but a very mild clinical phenotype [3-8]. We performed splicing experiments and computational structural analyses to investigate the role of the novel @entity73170 variant. Alamut software data predicted loss of splicing enhancers for the @entity73170 and @entity73171 mutations [9,10]. A cDNA library was generated from our @entity1 * s RNA to investigate for splicing errors, but no change in transcript length was seen [3]. In silico structural analysis was performed to investigate enzyme stability and attempt to understand the mechanism of the @entity1624 phenotype. Stability results are publicly available in the @entity29272 Protein Database 2.0 [11-14]. Animations were created to give the reader a dynamic view of the enzyme structure and mutation locations. Protein database files and python scripts are included for further investigation.
