1iu1

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(New page: 200px<br /> <applet load="1iu1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1iu1, resolution 1.80&Aring;" /> '''Crystal structure o...)
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Revision as of 15:28, 12 November 2007

Image:1iu1.gif

1iu1, resolution 1.80Å

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Crystal structure of human gamma1-adaptin ear domain

Overview

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.

About this Structure

1IU1 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural basis for the accessory protein recruitment by the gamma-adaptin ear domain., Nogi T, Shiba Y, Kawasaki M, Shiba T, Matsugaki N, Igarashi N, Suzuki M, Kato R, Takatsu H, Nakayama K, Wakatsuki S, Nat Struct Biol. 2002 Jul;9(7):527-31. PMID:12042876

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