 | Figure 2
Nature Structural Biology
9, 527 - 531 (2002)
Published online: 3 June 2002; | doi:10.1038/nsb808
Structural basis for the accessory protein recruitment by the  -adaptin ear domainTerukazu Nogi, Yoko Shiba, Masato Kawasaki, Tomoo Shiba, Naohiro Matsugaki, Noriyuki Igarashi, Mamoru Suzuki, Ryuichi Kato, Hiroyuki Takatsu, Kazuhisa Nakayama
& Soichi Wakatsuki | | | | Figure 2. Structure of the  -adaptin ear and  2-adaptin ear domains.
a, Ribbon diagram of the mouse  -adaptin ear domain (PDB entry 1B9K). b, Ribbon diagram of the human  2-adaptin ear domain (PDB entry 1E42). In addition to the N-terminal immunoglobulin (Ig)-like subdomain (yellow), the and 2 ear domains possess the C-terminal platform subdomain (blue). In terms of the C trace, the  1 ear domain is more similar to the ear domain than the 2 ear domain, which is consistent with the observation that 1-adaptin of the AP-1 complex is the counterpart of -adaptin of AP-2. The and 1 ear domains superimpose with an r.m.s. deviation of 1.1 Å for the 57 C atoms in the 8 -strands. R.m.s. deviations in the structure superposition were calculated using LSQKAB23. In the ear domain, the C-terminal subdomain serves as the recruitment platform for accessory proteins. A shallow hydrophobic binding pocket is located at the top of the platform subdomain (the magenta dotted circle in (a)).
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