In Depth Variant Analysis:  c.959T>C (p.Leu320Pro)
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c.959T>C
p.Leu320Pro (Legacy AA No. 302)
Variant Type:  
Point
Domain:  
Apple 4
Codon Change: 
T>C
Variant Effect: 
Missense
No. of Patients Reported: 
0
Phenotype: 
I
Allele Count *: 
-
Allele Number *: 
-
Allele Frequency *: 
-
Variant Comments & Reference:
Amount of mutant protein secreted from cells in vitro is reduced. Leu320 occurs adjacent to Cys321, which forms a disulfide bond with Cys327. Structural predictions indicate that the substitution of Pro for Leu320 causes the helical conformation at Cys317, Gln318, and Lys319 of the normal protein to be changed to turn and coil conformations. These changes in protein conformation might prevent the formation of the Cys321- Cys327 disulfide bond, altering the structure of the fourth apple domain. Pugh et al 1995Residue Information:
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Substitution Analysis:
Structural Implications:
Leu320 is an exposed residue  (surface accessibility value = 3 ).
Leu320 is in a region of secondary structure within the FXI domains.
The DSSP assignment for this residue is ... H.
Leu320 is in a region of secondary structure within the FXI domains.
The DSSP assignment for this residue is ... H.
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