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Novel Y283C mutation of the A subunit for coagulation factor XIII: molecular modelling predicts its impaired protein folding and dimer formation
Author(s) -
Souri Masayoshi,
Yee Vivien C.,
Kasai Kenichiro,
Kaneshiro Takashi,
Narasaki Kakutaro,
Castaman Giancarlo,
Ichinose Akitada
Publication year - 2001
Publication title -
british journal of haematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.907
H-Index - 186
eISSN - 1365-2141
pISSN - 0007-1048
DOI - 10.1046/j.1365-2141.2001.02797.x
Subject(s) - mutant , protein subunit , proband , mutation , microbiology and biotechnology , exon , genetics , dimer , polymerase chain reaction , restriction fragment length polymorphism , chemistry , biology , gene , organic chemistry
In an Italian patient with severe factor XIII deficiency, a novel mutation, Y283C (TAT to TGT), was identified heterozygously by nucleotide sequencing analysis in exon VII of the gene for the A subunit. The presence of this mutation was confirmed using polymerase chain reaction‐restriction fragment length polymorphism (PCR‐RFLP) analysis in the proband and his brother. Molecular modelling predicts that the mutant molecule would be misfolded. It is probable that the impaired folding of the mutant Y283C A subunit led to its instability, which is at least in part responsible for the factor XIII deficiency of this patient.