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Fig. 3 | Journal of Translational Medicine

Fig. 3

From: Assessing the genetic burden of familial hypercholesterolemia in a large middle eastern biobank

Fig. 3

Mapping of key regions in the 3D structure of PCSK9 and LDLR. A) Structure of PCSK9 showing arrangement of functional domains, pro-domain (brown), catalytic domain (gray) and cystine and histidine-rich domain (CHRD, cyan). (B-D) Zoomed in view of the domains [(B) pro-domain, (C) catalytic domain (D) CHRD (also binding region for annexin A2)] with labels. E) Structure of a PCSK9-LDLR complex shown with an epidermal growth factor (EGF) domain composed of EGF_A (purple), EGF_B (forest), EGF_C (orange) and β-propeller regions (slate). F) Zoomed in view of the β-propeller with neighbor domains. In this figure, positions are mapped and colored as follows: novel mutations, blue spheres; known mutations, yellow; catalytic triad, magenta; substrate binding region, pink; LDLR (EGF_A) binding region in PCSK9, green; allosteric inhibitor site, red

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