Skip to main content
. 2016 Jul 7;99(1):236–245. doi: 10.1016/j.ajhg.2016.05.026

Figure 2.

Figure 2

KLHL7 Protein Structure and In Silico Analysis of the Mutants Found in CS/CISS1 Phenotype

(A) Schematic representation of the KLHL7 protein. Substitutions reported here and in Friedman et al.16 are indicated. The corresponding positions are referred to the KLHL7 splice isoform 1.

(B) Protein alignment of the KLHL7 KELCH domain. All substitutions are marked in red with an asterisk. Position indicated as follows: asterisk (∗), identical; colon (:), strongly conserved; period (.), conserved; stabilized loops underlined. Sequence data used from Uniprot: human, Q8IXQ5; bovine (Bos taurus), Q0VCQ5; frog (Xenopus tropicalis), F6UPT8; bird (Gallus gallus), Q5ZI33; fly (Musca domestica), T1PLA9; worm (Caenorhabditis remanei), E3MGH6; plant (Oryza sativa), Q84S70; KEAP1: human Kelch-like ECH-associated protein 1, Q14145.

(C) Structure of human KLHL7 Kelch domain (PDB: 3II7) in schematic representation with substitutions p.Arg372Gln and p.Arg420Cys involved in salt bridges (stabilized loops in dark green); p.Cys421Ser with partial exposition to the solvent.