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1.
Figure 1

Figure 1. From: INVERTED FORMIN 2 MUTATIONS WITH VARIABLE EXPRESION IN PATIENTS WITH SPORADIC AND HEREDITARY FOCAL AND SEGMENTAL GLOMERULOSCLEROSIS.

New INF2 mutations in familial FSGS. (A) Protein domains of INF2. (B) The three new mutations detected in families with FSGS. The new mutations (E184Q, N202D, and A203D) are all missense mutations in exon 4 of the gene which encode for the diaphanous inhibitory domain (DID) of the protein. Note that the new variant N183K identified in this study is not conserved in evolution and is therefore not likely to be disease causing. (C) Normal sequences (D) The three new mutations and the other four mutations identified in this cohort are well conserved in evolution down to the zebra fish. *Denotes new mutations.

Rasheed Gbadegesin, et al. Kidney Int. ;81(1):94-99.
2.
Figure 2

Figure 2. From: INVERTED FORMIN 2 MUTATIONS WITH VARIABLE EXPRESION IN PATIENTS WITH SPORADIC AND HEREDITARY FOCAL AND SEGMENTAL GLOMERULOSCLEROSIS.

Renal biopsy in INF2 mutation and location of INF2 mutations in three dimensional modeling of INF2 DID based on structure of mDia1
Light microscopy of renal biopsies from two individuals with R177H and A203D showed segmental sclerosis with adhesions to Bowman’s capsule (Figures 2A–D). The biopsy from the individual with the R177H variant showed collapsing appearance in some glomeruli (Figures 2A and 2B). A model of human INF2 amino acids 1–330 was constructed using the Phyre threading server and the mDia1 structure (Figures 2E–F) (20). The region corresponding to the mDia1 IQGAP1 interacting DID subdomain (INF2 amino acids 149 through 238) is colored yellow13,21. New mutations identified in the present study are shown in blue, mutations identified in previous studies are shown in red8,13. (E) Global front view of the INF2 model. Residues N202 and A203 model to the protein surface next to I152, a residue identified as important for direct interaction with DAD (8, 13). (F) Global rear view of the INF2 model. Residue E184 maps to the surface of the protein and is adjacent to the previously identified mutation in S186.

Rasheed Gbadegesin, et al. Kidney Int. ;81(1):94-99.

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