1b9k

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[[Image:1b9k.gif|left|200px]]
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{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1b9k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b9k OCA], [http://www.ebi.ac.uk/pdbsum/1b9k PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1b9k RCSB]</span>
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'''ALPHA-ADAPTIN APPENDAGE DOMAIN, FROM CLATHRIN ADAPTOR AP2'''
'''ALPHA-ADAPTIN APPENDAGE DOMAIN, FROM CLATHRIN ADAPTOR AP2'''
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[[Category: Evans, P R.]]
[[Category: Evans, P R.]]
[[Category: Owen, D J.]]
[[Category: Owen, D J.]]
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[[Category: adaptor]]
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[[Category: Adaptor]]
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[[Category: endocytosis]]
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[[Category: Endocytosis]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:56:25 2008''
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Revision as of 08:14, 2 May 2008

Template:STRUCTURE 1b9k

ALPHA-ADAPTIN APPENDAGE DOMAIN, FROM CLATHRIN ADAPTOR AP2


Overview

The alpha subunit of the endocytotic AP2 adaptor complex contains a 30 kDa "appendage" domain, which is joined to the rest of the protein via a flexible linker. The 1.9 A resolution crystal structure of this domain reveals a single binding site for its ligands, which include amphiphysin, Eps15, and epsin. This domain when overexpressed in COS7 fibroblasts is shown to inhibit transferrin uptake, whereas mutants in which interactions with its binding partners are abolished do not. DPF/W motifs present in appendage domain-binding partners are shown to play a crucial role in their interactions with the domain. A single site for binding multiple ligands would allow for temporal and spatial regulation in the recruitment of components of the endocytic machinery.

About this Structure

1B9K is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

A structural explanation for the binding of multiple ligands by the alpha-adaptin appendage domain., Owen DJ, Vallis Y, Noble ME, Hunter JB, Dafforn TR, Evans PR, McMahon HT, Cell. 1999 Jun 11;97(6):805-15. PMID:10380931 Page seeded by OCA on Fri May 2 11:14:41 2008

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