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. 2019 Jul 24;22(1):150–159. doi: 10.1038/s41436-019-0606-y

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© The Author(s) 2019

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 2 — In silico modeling of DHX37 RecA1 and RecA2 pathogenic variants. (a) Functional domains of a homology model of DHX37 protein with U₇-RNA (dark blue) and a nonhydrolyzable adenosine triphosphate (ATP) analog (ADP-BeF_3, spheres). Domains are color-coded and labeled, conserved motifs are specified in circles, and the five disease-associated variants are indicated. The protein has four functional domains: two RecA-like domains, which are the helicase domains (RecA1: ATP-binding DEAH-box helicase, yellow, RecA2: C-terminal helicase, green); helicase associated 2 domain (HA2, red); and oligonucleotide/oligosaccharide-binding like domain (OB, pink). (b) Schematic diagram of the RecA-like domains in DEAH-box RNA helicases. Colors represent main helicase functions. Alignment of human (top) and Saccharomyces cerevisiae (bottom) showing the positions of recurrent variants causing 46,XY disorders/differences of sex development (DSD) with the consensus sequence shown in the middle. (c) Zoomed-in view of residue 308 and 334 with single-stranded RNA. (d) Residues 626 and 674 are shown to interact with the ATP analog. (e) Residue 304 is highlighted to be buried with a pocket within the RecA1 domain. Dashed lines within figure parts are shown for selected noncovalent polar interactions.