1qtp
From Proteopedia
(New page: 200px<br /><applet load="1qtp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qtp, resolution 1.60Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1qtp.jpg|left|200px]]<br /><applet load="1qtp" size=" | + | [[Image:1qtp.jpg|left|200px]]<br /><applet load="1qtp" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1qtp, resolution 1.60Å" /> | caption="1qtp, resolution 1.60Å" /> | ||
'''CRYSTAL STRUCTURE OF THE AP-2 CLATHRIN ADAPTOR ALPHA-APPENDAGE'''<br /> | '''CRYSTAL STRUCTURE OF THE AP-2 CLATHRIN ADAPTOR ALPHA-APPENDAGE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | AP-2 adaptors regulate clathrin-bud formation at the cell surface by | + | 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== | ==About this Structure== | ||
| - | 1QTP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http:// | + | 1QTP is a [http://en.wikipedia.org/wiki/Single_protein 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== | ||
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[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Downs, M | + | [[Category: Downs, M A.]] |
| - | [[Category: Fremont, D | + | [[Category: Fremont, D H.]] |
| - | [[Category: Traub, L | + | [[Category: Traub, L M.]] |
| - | [[Category: Westrich, J | + | [[Category: Westrich, J L.]] |
[[Category: four-wavelength mad]] | [[Category: four-wavelength mad]] | ||
[[Category: membrane protein]] | [[Category: membrane protein]] | ||
[[Category: selenomethionine]] | [[Category: selenomethionine]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:43:34 2008'' |
Revision as of 12:43, 21 February 2008
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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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