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. Author manuscript; available in PMC: 2016 Jul 13.
Published in final edited form as: JCI Insight. 2016 Jun 16;1(9):e86177. doi: 10.1172/jci.insight.86177

Figure 4. Structural modeling of NPHS1 and NEPH1 based on their homology to TITIN.

Figure 4

(A) Length distribution of individual strands within mouse foot processes in PET reconstructions gives 2 gaussian-like distributions centered at 45 nm and 23 nm. (B) For mouse NPHS1, databases (uniprot: Q9QZS7, ncbi: NP_062332.2) predict 8 N-terminal immunoglobulin type C2 domains and 1 C-terminal fibronectin type III domain. A ninth Ig domain (between Ig6 and Ig7, aa 650–753) was predicted with sequence alignments of all mouse NPHS1 Ig domains and with the use of PHYRE2 (36). Straight length for NEPHRIN was estimated at 43.8 nm. (C) In accordance with the literature, mouse NEPH1 (uniprot Q80W68, ncbi: NM_019459.2) consists of 5 N-terminal immunoglobulin type C2 domains. In the case of NEPH1, straight length was estimated to be 19.7 nm.