In Depth Variant Analysis:  c.1718G>A (p.Gly573Glu)
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c.1718G>A
p.Gly573Glu (Legacy AA No. 555)
Variant Type:  
Point
Domain:  
Serine Protease
Codon Change: 
G>A
Variant Effect: 
Missense
No. of Patients Reported: 
2
Phenotype: 
II
Allele Count *: 
2
Allele Number *: 
251370
Allele Frequency *: 
0.000008
Variant Comments & Reference:
Normal amount of mutant protein secreted from BHK cells. Experimental data indicates the mutation changes the conformation of the unoccupied active site of FXIa. When compared with wild type, FXI-Glu573 activates FIX at a greatly reduced rate. Modelling indicates side chain of Glu573 alters electrostatic charge around active site and interferes with the interaction between FXI and FIX and antithrombin. Zivelin et al 2001 (Abstract), Zivelin et al 2004, Schmidt et al 2004Residue Information:
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Substitution Analysis:
Structural Implications:
Gly573 is a buried residue  (surface accessibility value = 1 ).
Gly573 is in a random coil area of the FXI structure.
The DSSP assignment for this residue is ... C.
Gly573 is in a random coil area of the FXI structure.
The DSSP assignment for this residue is ... C.
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