Fig 1: CCDC22 and CCDC93 linkers make extensive contacts with the central COMM domain ring and peripheral HN domains, related to Figure 4(A) Details of the five interfaces between the COMMD heterodimers of the heterodecameric ring. The central schematic is as shown in Figure 4D to provide a reference for each interface. Structural panels show adjacent heterotetramers in the same orientation, placing the strictly conserved Trp sidechain of each subunit as the focal point. Many specific interactions between adjacent subunits determine the precise COMMD organization.(B and C) Interfaces between CCDC22 and the HN of COMMD3 and COMMD8, and (C) between CCDC93 and HN domains of COMMD2 and COMMD4.
Fig 2: CryoEM structure of the human CCC complex(A) CryoEM structure of the CCC complex revealing the COMMD proteins, the CH domain of CCDC93, and linker regions of CCDC22 and CCDC93. Linker domains of CCDC22 and CCDC93 visible in our cryoEM map form intricate interactions with the decameric COMMD structure, leading to a highly intertwined structure. The CH domain of CCDC22 and extended coiled-coil regions of the CCDC proteins are not visible in current cryoEM maps due to flexibility relative to the stable COMMD decamer.(B) Molecular surface highlighting the organization of the HN domains of COMMD1, 4, 2, 10, and 7 on one side of the COMM domain ring, and COMMD8, 3, 5, and 9 on the other side. Human COMMD6 lacks the HN domain. For clarity, CCDC22 and CCDC93 are omitted.(C) Schematic model of COMMD decamer and arrangement of the sub-complexes.(D) Interweaving of CCDC22 and CCDC93 within the COMMD ring.(E) Interactions stabilizing the CCDC93 CH domain contact with the central COMMD ring, via the HN domain of COMMD4.(F and G) The PxxR sequences in CCDC22 that form turn structures: (F) the 145PHLR148 motif binds the HN domain of COMMD5; and (G) the 199 PVGR202 motif binds the COMMD3 HN domain.See also Figures S2, S3, S4, and S5.
Supplier Page from Abcam for Anti-COMMD3 antibody