Components of Coated Vesicles and Nuclear Pore Complexes Share a Common Molecular Architecture (original) (raw)
Figure 4
The Nup84 Complex and Coated Vesicles Share a Common Architecture
A diagram showing the organization of the clathrin/AP-2 coated vesicle complex is shown at left; the positions of clathrin and the adaptin AP-2 large subunits (α, β2 plus “ear” domains) and small subunits (σ, μ) are indicated. β-propeller regions are colored cyan, α-solenoid regions are colored magenta, and sample ribbon models for each fold are shown in the center. The variants of each fold that are found as domains in major components of the three kinds of vesicle-coating complexes and the yNup84 subcomplex are listed on the right. The -N and -C indicate amino-terminal and carboxyl-terminal domains, respectively. The classification of these domains is based on X-ray crystallography data (clathrin, α-adaptin, β2-adaptin [PDB codes 1gw5, 1bpo, 1b89 (ter Haar et al. 1998; Collins et al. 2002)]), by the detailed homology modeling presented here (yNup84 complex proteins; ySec13 also in Saxena et al. [1996]), or by sequence homology or unpublished secondary structure prediction and preliminary analyses (COPI I (sec31) complex proteins [Schledzewski et al. 1999], Sec31).