Factor VII C329R: a variant with a disrupted disulfide bond in the catalytic domain.
We report a novel mutation within the coagulation factor VII gene associated with a dysfunctional procoagulant factor VII (12% of normal plasma factor VII activity; 50% of normal plasma factor VII antigen level). Using heteroduplex analysis and subsequent sequencing, we identified a thymine-10,902 to cytosine mutation within exon eight of the factor VII gene, encoding for a substitution of arginine for cysteine-329 (factor VII C329R) within the heavy chain of factor VII. This substitution disrupts a disulfide bond within the factor VII catalytic domain and might cause altered conformation of the active site triad.
James
H L
HL
Department of Biochemistry, The University of Texas Health Center at Tyler, 75710, USA. hal@uthct.edu
Anderson
K D
KD
Nichols
W L
WL
Heit
J A
JA
D003596:Cytosine; D005167:Factor VII / Q000737:chemistry / Q000235:genetics*; D006801:Humans; D008297:Male; D008875:Middle Aged; D009154:Mutation; D011487:Protein Conformation; D013941:Thymine
D003596:Cytosine; D005167:Factor VII; D013941:Thymine