1w63

AP1 clathrin adaptor core

spinqualitylabelsall models 1w63, resolution 4.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1w63 is a 24 chain structure with sequence from Mus musculus and Rattus norvegicus. The April 2007 RCSB PDB Molecule of the Month feature on Clathrin by Graham T. Johnson and David S. Goodsell is 10.2210/rcsb_pdb/mom_2007_4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 4Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function AP1G1_MOUSE Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Adaptin 3D structures

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