1IU1

Crystal structure of human gamma1-adaptin ear domain

Summary for 1IU1

• Entry DOI: 10.2210/pdb1iu1/pdb
• Descriptor: gamma1-adaptin (2 entities in total)
• Functional Keywords: coated pits, endocytosis
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 32270.53

Authors

Nogi, T.,Shiba, Y.,Kawasaki, M.,Shiba, T.,Matsugaki, N.,Igarashi, N.,Suzuki, M.,Kato, R.,Takatsu, H.,Nakayama, K.,Wakatsuki, S. (deposition date: 2002-02-19, release date: 2002-07-10, Last modification date: 2023-12-27)

Primary citation

Nogi, T.,Shiba, Y.,Kawasaki, M.,Shiba, T.,Matsugaki, N.,Igarashi, N.,Suzuki, M.,Kato, R.,Takatsu, H.,Nakayama, K.,Wakatsuki, S.
Structural basis for the accessory protein recruitment by the gamma-adaptin ear domain.
Nat.Struct.Biol., 9:527-531, 2002

PubMed Abstract: The adaptor proteins AP-1 and GGA regulate membrane traffic between the trans-Golgi network (TGN) and endosomes/lysosomes through ARF-regulated membrane association, recognition of sorting signals, and recruitment of clathrin and accessory proteins. The gamma 1-adaptin subunits of AP-1 and GGA possess homologous ear domains involved in the recruitment of accessory proteins, gamma-synergin and Rabaptin-5. The crystal structure of the human gamma 1-adaptin ear domain consists solely of an immunoglobulin-like fold, unlike the alpha-adaptin ear domain. Structure-based mutational analyses reveal a binding site for the accessory proteins that is composed of conserved basic residues, indicating that the recruitment mechanism in gamma 1-adaptin and GGA is distinct from that in alpha-adaptin.

PubMed: 12042876
DOI: 10.1038/nsb808

Experimental method

X-RAY DIFFRACTION (1.8 Å)