1iu1: Difference between revisions

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[[Image:1iu1.jpg|left|200px]]
{{Seed}}
[[Image:1iu1.png|left|200px]]


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{{STRUCTURE_1iu1|  PDB=1iu1  |  SCENE=  }}  
{{STRUCTURE_1iu1|  PDB=1iu1  |  SCENE=  }}  


'''Crystal structure of human gamma1-adaptin ear domain'''
===Crystal structure of human gamma1-adaptin ear domain===




==Overview==
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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.
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{{ABSTRACT_PUBMED_12042876}}


==About this Structure==
==About this Structure==
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[[Category: Coated pit]]
[[Category: Coated pit]]
[[Category: Endocytosis]]
[[Category: Endocytosis]]
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