1w63 | pdb_00001w63
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AP1 CLATHRIN ADAPTOR CORE
Overview
The heterotetrameric adaptor proteins (AP complexes) link the outer, lattice of clathrin-coated vesicles with membrane-anchored cargo, molecules. We report the crystal structure of the core of the AP-1, complex, which functions in the trans-Golgi network (TGN). Packing of, complexes in the crystal generates an exceptionally long (1,135-A), unit-cell axis, but the 6-fold noncrystallographic redundancy yields an, excellent map at 4-A resolution. The AP-1 core comprises N-terminal, fragments of the two large chains, beta1 and gamma, and the intact medium, and small chains, micro1 and sigma1. Its molecular architecture closely, resembles that of the core of AP-2, the plasma-membrane-specific adaptor, for which a structure has been determined. Both structures represent an, "inactive" conformation with respect to binding of cargo with a, tyrosine-based sorting signal. TGN localization of AP-1 depends on the, small GTPase, Arf1, and the phosphoinositide, PI-4-P. We show that, directed mutations of residues at a particular corner of the gamma chain, prevent recruitment to the TGN in cells and diminish PI-4-P-dependent, but, not Arf1-dependent, liposome binding in vitro.
About this Structure
1W63 is a Protein complex structure of sequences from Mus musculus and Rattus norvegicus. The following page contains interesting information on the relation of 1W63 with [Clathrin]. Full crystallographic information is available from OCA.
Reference
Crystal structure of the clathrin adaptor protein 1 core., Heldwein EE, Macia E, Wang J, Yin HL, Kirchhausen T, Harrison SC, Proc Natl Acad Sci U S A. 2004 Sep 28;101(39):14108-13. Epub 2004 Sep 17. PMID:15377783
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