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Table 1 Structural deviation in the backbone torsion angles of the wild type and mutated human FZD4 proteins

From: Molecular evolutionary and structural analysis of familial exudative vitreoretinopathy associated FZD4 gene

Comparison of wild-type and mutated structures

Major change in backbone torsion angles (residue number)

Major shift in regions

Critical region

P33S

44,45,110,132-135,137,141-143,147–150

CRD domain

 

285,417–432

Seven TMs domain.

 

496–537

K-T-XXX-W, PDZ binding motif

 

G36D

41–46,70,71,133-138,141–150

CRD domain

 

416–431,468

Seven TMs domain.

 

495–537

K-T-XXX-W, PDZ binding motif

 

E40Q

135–144,156–158

CRD domain

 

182–186,199, 202

UCR

 

243–244,248,284-286,337-338,417-420,466–469

Seven TMs domain

 

505–537

PDZ binding motif

 

Y58C

134–135,141-144,147–150

CRD domain

 

243–244,248,284-285,334-337,416-431,467-469,495–497

Seven TMs domain

 

508–537

PDZ binding motif

 

H69Y

147–149

CRD domain

 

285,287,334-339,415–432

Seven TMs domain

 

504–537

K-T-XXX-W, PDZ binding motif

 

M105 T

274–278,284-286,467,468

Seven TMs domain

 

506–537

PDZ binding motif

495–537

M105 V

107–114,132–135

CRD domain

 

284–286,332-338,416-430,467–469.

Seven TMs domain

 

505–537

PDZ binding motif

 

I114T

15–44,49,62-81,110,118,134–156

Signal peptide and CRD domain

 

213–214,274–275

Seven TMs domain

 

495–537

K-T-XXX-W, PDZ binding motif

 

C117R

49,70-71,73–74

CRD domain

 

274–275

Seven TMs domain

 

496–537

K-T-XXX-W, PDZ binding motif

 

R127H

15–44,49,63-81,110-111,118,133–156

Signal peptide and CRD domain

 

173–179

UCR

 

213–214,274–275

Seven TMs domain

 

496–537

K-T-XXX-W, PDZ binding motif

 

M157 V

133–135,142–151

CRD domain

 

284,285,337,338,417-423,428-431,467–470

Seven TMs domain

 

496–537

K-T-XXX-W, PDZ binding motif

 

C181R

419–422

Seven TMs domain

 

503–537

PDZ binding motif

 

C181Y

420–423

Seven TMs domain

 

508–537

PDZ binding motif

 

C204R

69–72,134,135,144–150

CRD domain

 

337,338,418-420,430,431

Seven TMs domain

 

495–537

K-T-XXX-W, PDZ binding motif

 

C204Y

66–67,70-71,102,141–150

CRD domain

 

243–244,419–420

Seven TMs domain

 

504–537

K-T-XXX-W, PDZ binding motif

 

Y211H

496–537

K-T-XXX-W, PDZ binding motif

 

M223K

504–537

K-T-XXX-W, PDZ binding motif

 

T237R

214,274–275

Seven TMs domain

 

503–537

K-T-XXX-W, PDZ binding motif

 

R253C

504–537

K-T-XXX-W, PDZ binding motif

 

W335C

274–275

Seven TMs domain

 

496–537

K-T-XXX-W, PDZ binding motif

 

A370G

46–52,68-80,141

CRD domain

 

504–537

K-T-XXX-W, PDZ binding motif

 

R417Q

42–46,147-150,134-137,147–150

CRD domain

 

418–432

Seven TMs domain

 

507–537

PDZ binding motif

 

G488D

41–46,109-114,133–151

CRD domain

 

416–432

Seven TMs domain

 

495–537

K-T-XXX-W, PDZ binding motif

 

G488 V

38,70

CRD domain

 

505–537

PDZ binding motif

 

S497F

70–71,73–74

CRD domain

 

503–537

K-T-XXX-W, PDZ binding motif

 

K499E

147–148

CRD domain

 

284–286, 336–338,418–431, 468–470

Seven TMs domain

 

505–537

K-T-XXX-W, PDZ binding motif

 
  1. This table shows the impact of FEVR associated missense mutations in the FZD4 protein on its backbone torsion angles by comparing them with its normal structure. The critical region encompasses the K-T-XXX-W and T/S-X-VPDZ binding motifs. In the first column, amino acid residue on the left indicates the wild-type residue; the number shows the amino acid position of the residue in the protein sequence, while the residue on the right shows the mutated residue. The second column specifies the positions at which major structural deviations were observed
  2. The third column depicts the deviated region/residues shared among all mutant proteins analyzed (critical region)
  3. CRD cysteine rich domain, TM transmembrane, UCR uncharacterized region
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BMC Ecology and Evolution

ISSN: 2730-7182

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