|
|
| Line 1: |
Line 1: |
| [[Image:1e42.gif|left|200px]] | | {{Seed}} |
| | [[Image:1e42.png|left|200px]] |
|
| |
|
| <!-- | | <!-- |
| Line 9: |
Line 10: |
| {{STRUCTURE_1e42| PDB=1e42 | SCENE= }} | | {{STRUCTURE_1e42| PDB=1e42 | SCENE= }} |
|
| |
|
| '''BETA2-ADAPTIN APPENDAGE DOMAIN, FROM CLATHRIN ADAPTOR AP2'''
| | ===BETA2-ADAPTIN APPENDAGE DOMAIN, FROM CLATHRIN ADAPTOR AP2=== |
|
| |
|
|
| |
|
| ==Overview==
| | <!-- |
| The heterotetrameric AP2 adaptor (alpha, beta 2, mu 2 and sigma 2 subunits) plays a central role in clathrin-mediated endocytosis. We present the protein recruitment function and 1.7 A resolution structure of its beta 2-appendage domain to complement those previously determined for the mu 2 subunit and alpha appendage. Using structure-directed mutagenesis, we demonstrate the ability of the beta 2 appendage alone to bind directly to clathrin and the accessory proteins AP180, epsin and eps15 at the same site. Clathrin polymerization is promoted by binding of clathrin simultaneously to the beta 2-appendage site and to a second site on the adjacent beta 2 hinge. This results in the displacement of the other ligands from the beta 2 appendage. Thus clathrin binding to an AP2-accessory protein complex would cause the controlled release of accessory proteins at sites of vesicle formation. | | The line below this paragraph, {{ABSTRACT_PUBMED_10944104}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 10944104 is the PubMed ID number. |
| | --> |
| | {{ABSTRACT_PUBMED_10944104}} |
|
| |
|
| ==About this Structure== | | ==About this Structure== |
| Line 27: |
Line 31: |
| [[Category: Adaptor]] | | [[Category: Adaptor]] |
| [[Category: Endocytosis]] | | [[Category: Endocytosis]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:38:15 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:07:04 2008'' |