1qtp
From Proteopedia
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| - | [[Image:1qtp.jpg|left|200px]] | + | [[Image:1qtp.jpg|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF THE AP-2 CLATHRIN ADAPTOR ALPHA-APPENDAGE''' | + | {{Structure |
| + | |PDB= 1qtp |SIZE=350|CAPTION= <scene name='initialview01'>1qtp</scene>, resolution 1.60Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''CRYSTAL STRUCTURE OF THE AP-2 CLATHRIN ADAPTOR ALPHA-APPENDAGE''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1QTP is a [ | + | 1QTP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QTP OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure of the alpha appendage of AP-2 reveals a recruitment platform for clathrin-coat assembly., Traub LM, Downs MA, Westrich JL, Fremont DH, Proc Natl Acad Sci U S A. 1999 Aug 3;96(16):8907-12. PMID:[http:// | + | Crystal structure of the alpha appendage of AP-2 reveals a recruitment platform for clathrin-coat assembly., Traub LM, Downs MA, Westrich JL, Fremont DH, Proc Natl Acad Sci U S A. 1999 Aug 3;96(16):8907-12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10430869 10430869] |
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: selenomethionine]] | [[Category: selenomethionine]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:42:35 2008'' |
Revision as of 11:42, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE AP-2 CLATHRIN ADAPTOR ALPHA-APPENDAGE
Overview
AP-2 adaptors regulate clathrin-bud formation at the cell surface by recruiting clathrin trimers to the plasma membrane and by selecting certain membrane proteins for inclusion within the developing clathrin-coat structure. These functions are performed by discrete subunits of the adaptor heterotetramer. The carboxyl-terminal appendage of the AP-2 alpha subunit appears to regulate the translocation of several endocytic accessory proteins to the bud site. We have determined the crystal structure of the alpha appendage at 1.4-A resolution by multiwavelength anomalous diffraction phasing. It is composed of two distinct structural modules, a beta-sandwich domain and a mixed alpha-beta platform domain. Structure-based mutagenesis shows that alterations to the molecular surface of a highly conserved region on the platform domain differentially affect associations of the appendage with amphiphysin, eps15, epsin, and AP180, revealing a common protein-binding interface.
About this Structure
1QTP is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Crystal structure of the alpha appendage of AP-2 reveals a recruitment platform for clathrin-coat assembly., Traub LM, Downs MA, Westrich JL, Fremont DH, Proc Natl Acad Sci U S A. 1999 Aug 3;96(16):8907-12. PMID:10430869
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